ID Q8WSF8_APLCA Unreviewed; 236 AA. AC Q8WSF8; DT 01-MAR-2002, integrated into UniProtKB/TrEMBL. DT 01-MAR-2002, sequence version 1. DT 10-FEB-2021, entry version 114. DE SubName: Full=Soluble acetylcholine receptor {ECO:0000313|EMBL:AAL37251.1}; OS Aplysia californica (California sea hare). OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda; OC Heterobranchia; Euthyneura; Euopisthobranchia; Aplysiida; Aplysioidea; OC Aplysiidae; Aplysia. OX NCBI_TaxID=6500 {ECO:0000313|EMBL:AAL37251.1}; RN [1] {ECO:0000213|PDB:2BYN, ECO:0000213|PDB:2BYP, ECO:0000213|PDB:2BYQ} RP X-RAY CRYSTALLOGRAPHY (2.02 ANGSTROMS) OF 18-236, GLYCOSYLATION AT ASN-91, RP AND DISULFIDE BONDS. RX PubMed=16193063; DOI=10.1038/sj.emboj.7600828; RA Hansen S.B., Sulzenbacher G., Huxford T., Marchot P., Taylor P., Bourne Y.; RT "Structures of Aplysia AChBP complexes with nicotinic agonists and RT antagonists reveal distinctive binding interfaces and conformations."; RL EMBO J. 24:3635-3646(2005). RN [2] {ECO:0000213|PDB:2BR7, ECO:0000213|PDB:2BR8} RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 20-236, AND DISULFIDE BONDS. RX PubMed=15951818; DOI=10.1038/nsmb951; RA Celie P.H., Kasheverov I.E., Mordvintsev D.Y., Hogg R.C., van Nierop P., RA van Elk R., van Rossum-Fikkert S.E., Zhmak M.N., Bertrand D., Tsetlin V., RA Sixma T.K., Smit A.B.; RT "Crystal structure of nicotinic acetylcholine receptor homolog AChBP in RT complex with an alpha-conotoxin PnIA variant."; RL Nat. Struct. Mol. Biol. 12:582-588(2005). RN [3] {ECO:0000313|EMBL:AAL37251.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=17190607; DOI=10.1016/j.cell.2006.09.052; RA Moroz L.L., Edwards J.R., Puthanveettil S.V., Kohn A.B., Ha T., Heyland A., RA Knudsen B., Sahni A., Yu F., Liu L., Jezzini S., Lovell P., Iannucculli W., RA Chen M., Nguyen T., Sheng H., Shaw R., Kalachikov S., Panchin Y.V., RA Farmerie W., Russo J.J., Ju J., Kandel E.R.; RT "Neuronal transcriptome of Aplysia: neuronal compartments and circuitry."; RL Cell 127:1453-1467(2006). RN [4] {ECO:0000213|PDB:2C9T} RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 20-236, AND DISULFIDE BONDS. RX PubMed=16505382; DOI=10.1073/pnas.0507889103; RA Ulens C., Hogg R.C., Celie P.H., Bertrand D., Tsetlin V., Smit A.B., RA Sixma T.K.; RT "Structural determinants of selective alpha-conotoxin binding to a RT nicotinic acetylcholine receptor homolog AChBP."; RL Proc. Natl. Acad. Sci. U.S.A. 103:3615-3620(2006). RN [5] {ECO:0000213|PDB:2UZ6} RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 20-236, AND DISULFIDE BONDS. RX PubMed=17660751; DOI=10.1038/sj.emboj.7601785; RA Dutertre S., Ulens C., Buttner R., Fish A., van Elk R., Kendel Y., RA Hopping G., Alewood P.F., Schroeder C., Nicke A., Smit A.B., Sixma T.K., RA Lewis R.J.; RT "AChBP-targeted alpha-conotoxin correlates distinct binding orientations RT with nAChR subtype selectivity."; RL EMBO J. 26:3858-3867(2007). RN [6] {ECO:0000213|PDB:2PGZ, ECO:0000213|PDB:2PH9} RP X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) OF 18-236, GLYCOSYLATION AT ASN-91, RP AND DISULFIDE BONDS. RX PubMed=17481657; DOI=10.1016/j.jmb.2007.03.067; RA Hansen S.B., Taylor P.; RT "Galanthamine and non-competitive inhibitor binding to ACh-binding protein: RT evidence for a binding site on non-alpha-subunit interfaces of heteromeric RT neuronal nicotinic receptors."; RL J. Mol. Biol. 369:895-901(2007). RN [7] {ECO:0000213|PDB:3GUA} RP X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 18-225, AND DISULFIDE BONDS. RX PubMed=18940802; DOI=10.1074/jbc.C800194200; RA Hansen S.B., Wang H.L., Taylor P., Sine S.M.; RT "An ion selectivity filter in the extracellular domain of Cys-loop RT receptors reveals determinants for ion conductance."; RL J. Biol. Chem. 283:36066-36070(2008). RN [8] {ECO:0000213|PDB:3C79, ECO:0000213|PDB:3C84} RP X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) OF 18-236, AND DISULFIDE BONDS. RX PubMed=18477694; DOI=10.1073/pnas.0802197105; RA Talley T.T., Harel M., Hibbs R.E., Radic Z., Tomizawa M., Casida J.E., RA Taylor P.; RT "Atomic interactions of neonicotinoid agonists with AChBP: molecular RT recognition of the distinctive electronegative pharmacophore."; RL Proc. Natl. Acad. Sci. U.S.A. 105:7606-7611(2008). RN [9] {ECO:0000213|PDB:2WN9, ECO:0000213|PDB:2WNC, ECO:0000213|PDB:2WNJ} RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 18-236, GLYCOSYLATION AT ASN-91, RP AND DISULFIDE BONDS. RX PubMed=19696737; DOI=10.1038/emboj.2009.227; RA Hibbs R.E., Sulzenbacher G., Shi J., Talley T.T., Conrod S., Kem W.R., RA Taylor P., Marchot P., Bourne Y.; RT "Structural determinants for interaction of partial agonists with RT acetylcholine binding protein and neuronal alpha7 nicotinic acetylcholine RT receptor."; RL EMBO J. 28:3040-3051(2009). RN [10] {ECO:0000213|PDB:2W8F, ECO:0000213|PDB:2W8G, ECO:0000213|PDB:2Y7Y} RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 20-236, AND DISULFIDE BONDS. RX PubMed=19331415; DOI=10.1021/jm801400g; RA Ulens C., Akdemir A., Jongejan A., van Elk R., Bertrand S., Perrakis A., RA Leurs R., Smit A.B., Sixma T.K., Bertrand D., de Esch I.J.; RT "Use of acetylcholine binding protein in the search for novel alpha7 RT nicotinic receptor ligands. In silico docking, pharmacological screening, RT and X-ray analysis."; RL J. Med. Chem. 52:2372-2383(2009). RN [11] {ECO:0000213|PDB:4ZJS} RP X-RAY CRYSTALLOGRAPHY (2.23 ANGSTROMS) OF 48-77 AND 99-236, AND DISULFIDE RP BONDS. RX PubMed=19890000; DOI=10.1523/JNEUROSCI.2833-09.2009; RA Luo J., Taylor P., Losen M., de Baets M.H., Shelton G.D., Lindstrom J.; RT "Main immunogenic region structure promotes binding of conformation- RT dependent myasthenia gravis autoantibodies, nicotinic acetylcholine RT receptor conformation maturation, and agonist sensitivity."; RL J. Neurosci. 29:13898-13908(2009). RN [12] {ECO:0000213|PDB:2WZY, ECO:0000213|PDB:2X00} RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 18-236, AND DISULFIDE BONDS. RX PubMed=20224036; DOI=10.1073/pnas.0912372107; RA Bourne Y., Radic Z., Araoz R., Talley T.T., Benoit E., Servent D., RA Taylor P., Molgo J., Marchot P.; RT "Structural determinants in phycotoxins and AChBP conferring high affinity RT binding and nicotinic AChR antagonism."; RL Proc. Natl. Acad. Sci. U.S.A. 107:6076-6081(2010). RN [13] {ECO:0000213|PDB:3PEO} RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 18-236, AND DISULFIDE BONDS. RA Talley T.T., Harel M., Yamauchi G.J., Radic Z., Hansen S., Huxford T., RA Taylor P.W.; RT "The curare alkaloids: analyzing the poses of complexes with the RT acetylcholine binding protein in relation to structure and binding RT energetics."; RL Submitted (OCT-2010) to the PDB data bank. RN [14] {ECO:0000213|PDB:3PMZ} RP X-RAY CRYSTALLOGRAPHY (2.44 ANGSTROMS) OF 18-236 IN COMPLEX WITH MAGNESIUM, RP AND DISULFIDE BONDS. RA Talley T.T., Harel M., Yamauchi J.G., Radic Z., Hansen S., Huxford T., RA Taylor P.W.; RT "The Curare Alkaloids: Analyzing the Poses of Complexes with the RT Acetylcholine Binding Protein in Relation to Structure and Binding RT Energies."; RL Submitted (NOV-2010) to the PDB data bank. RN [15] {ECO:0000213|PDB:2XNT, ECO:0000213|PDB:2XNU, ECO:0000213|PDB:2XNV} RP X-RAY CRYSTALLOGRAPHY (2.44 ANGSTROMS), AND DISULFIDE BONDS. RX PubMed=21920761; DOI=10.1016/j.bmc.2011.08.028; RA Akdemir A., Rucktooa P., Jongejan A., Elk R.v., Bertrand S., Sixma T.K., RA Bertrand D., Smit A.B., Leurs R., de Graaf C., de Esch I.J.; RT "Acetylcholine binding protein (AChBP) as template for hierarchical in RT silico screening procedures to identify structurally novel ligands for the RT nicotinic receptors."; RL Bioorg. Med. Chem. 19:6107-6119(2011). RN [16] {ECO:0000213|PDB:2Y54, ECO:0000213|PDB:2Y56, ECO:0000213|PDB:2Y57} RP X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS) OF 20-236, AND DISULFIDE BONDS. RX PubMed=21322593; DOI=10.1021/ja110571r; RA Edink E., Rucktooa P., Retra K., Akdemir A., Nahar T., Zuiderveld O., RA van Elk R., Janssen E., van Nierop P., van Muijlwijk-Koezen J., Smit A.B., RA Sixma T.K., Leurs R., de Esch I.J.; RT "Fragment growing induces conformational changes in acetylcholine-binding RT protein: a structural and thermodynamic analysis."; RL J. Am. Chem. Soc. 133:5363-5371(2011). RN [17] {ECO:0000213|PDB:2XZ5, ECO:0000213|PDB:2XZ6} RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 20-236, AND DISULFIDE BONDS. RX PubMed=21115477; DOI=10.1074/jbc.M110.188730; RA Brams M., Gay E.A., Saez J.C., Guskov A., van Elk R., van der Schors R.C., RA Peigneur S., Tytgat J., Strelkov S.V., Smit A.B., Yakel J.L., Ulens C.; RT "Crystal structures of a cysteine-modified mutant in loop D of RT acetylcholine-binding protein."; RL J. Biol. Chem. 286:4420-4428(2011). RN [18] {ECO:0000213|PDB:3SH1, ECO:0000213|PDB:3SIO, ECO:0000213|PDB:3T4M} RP X-RAY CRYSTALLOGRAPHY (2.32 ANGSTROMS) OF 18-236, GLYCOSYLATION AT ASN-91, RP AND DISULFIDE BONDS. RX PubMed=22009746; DOI=10.1074/jbc.M111.286583; RA Nemecz A., Taylor P.; RT "Creating an alpha7 nicotinic acetylcholine recognition domain from the RT acetylcholine-binding protein: crystallographic and ligand selectivity RT analyses."; RL J. Biol. Chem. 286:42555-42565(2011). RN [19] {ECO:0000213|PDB:2XYS, ECO:0000213|PDB:2XYT} RP X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) OF 20-236, AND DISULFIDE BONDS. RX PubMed=21468359; DOI=10.1371/journal.pbio.1001034; RA Brams M., Pandya A., Kuzmin D., van Elk R., Krijnen L., Yakel J.L., RA Tsetlin V., Smit A.B., Ulens C.; RT "A structural and mutagenic blueprint for molecular recognition of RT strychnine and d-tubocurarine by different cys-loop receptors."; RL PLoS Biol. 9:e1001034-e1001034(2011). RN [20] {ECO:0000213|PDB:4DBM} RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 18-236, GLYCOSYLATION AT ASN-91, RP AND DISULFIDE BONDS. RX PubMed=22394239; DOI=10.1021/ja3001858; RA Grimster N.P., Stump B., Fotsing J.R., Weide T., Talley T.T., RA Yamauchi J.G., Nemecz A., Kim C., Ho K.Y., Sharpless K.B., Taylor P., RA Fokin V.V.; RT "Generation of candidate ligands for nicotinic acetylcholine receptors via RT in situ click chemistry with a soluble acetylcholine binding protein RT template."; RL J. Am. Chem. Soc. 134:6732-6740(2012). RN [21] {ECO:0000213|PDB:4AFT, ECO:0000213|PDB:4BQT} RP X-RAY CRYSTALLOGRAPHY (2.88 ANGSTROMS) OF 20-236, AND DISULFIDE BONDS. RX PubMed=22553201; DOI=10.1074/jbc.M112.360347; RA Rucktooa P., Haseler C.A., van Elk R., Smit A.B., Gallagher T., Sixma T.K.; RT "Structural characterization of binding mode of smoking cessation drugs to RT nicotinic acetylcholine receptors through study of ligand complexes with RT acetylcholine-binding protein."; RL J. Biol. Chem. 287:23283-23293(2012). RN [22] {ECO:0000213|PDB:4EZ1} RP X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) OF 18-236, AND DISULFIDE BONDS. RA Filchakova O.M., Talley T.T., Reger A.S., Kim C., Ho K., Han K., Taylor P., RA McIntosh J.M.; RT "Pairwise interaction of alpha-conotoxin BuIA Pro6 with the beta subunit of RT nicotinic acetylcholine receptor."; RL Submitted (MAY-2012) to the PDB data bank. RN [23] {ECO:0000213|PDB:4FRR} RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 18-225, AND DISULFIDE BONDS. RA Mukhopadhyay S., Mesecar A.D.; RT "X-ray structure of Acetylcholine binding protein from Aplysia californica RT in presence of 3-((S)-azetidin-2-ylmethoxy)-5-((1S,2R)-2-(2- RT methoxyethyl)cyclopropyl)pyridine."; RL Submitted (JUN-2012) to the PDB data bank. RN [24] {ECO:0000213|PDB:2YMD, ECO:0000213|PDB:2YME} RP X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) OF 20-231, GLYCOSYLATION AT ASN-91, RP AND DISULFIDE BONDS. RX PubMed=23196367; DOI=10.1038/embor.2012.189; RA Kesters D., Thompson A.J., Brams M., van Elk R., Spurny R., Geitmann M., RA Villalgordo J.M., Guskov A., Danielson U.H., Lummis S.C., Smit A.B., RA Ulens C.; RT "Structural basis of ligand recognition in 5-HT3 receptors."; RL EMBO Rep. 14:49-56(2013). RN [25] {ECO:0000213|PDB:4BFQ} RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 20-236, AND DISULFIDE BONDS. RX PubMed=23695669; DOI=10.1038/NCOMMS2900; RA Stornaiuolo M., De Kloe G.E., Rucktooa P., Fish A., van Elk R., Edink E.S., RA Bertrand D., Smit A.B., de Esch I.J., Sixma T.K.; RT "Assembly of a pi-pi stack of ligands in the binding site of an RT acetylcholine-binding protein."; RL Nat. Commun. 4:1875-1875(2013). RN [26] {ECO:0000213|PDB:4WV9} RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 18-224, AND DISULFIDE BONDS. RA Talley T.T.; RT "Crystal structure of acetylcholine binding protein (AChBP) from Aplysia RT Californica in complex with click chemistry compound."; RL Submitted (NOV-2014) to the PDB data bank. RN [27] {ECO:0000213|PDB:5AIN} RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 20-231, AND DISULFIDE BONDS. RX PubMed=25648658; DOI=10.1021/CN500369H; RA Price K.L., Lillestol R.K., Ulens C., Lummis S.C.; RT "Varenicline Interactions at the 5-HT3 Receptor Ligand Binding Site are RT Revealed by 5-HTBP."; RL ACS Chem. Neurosci. 6:1151-1157(2015). RN [28] {ECO:0000213|PDB:4XHE, ECO:0000213|PDB:4XK9} RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 18-225, AND DISULFIDE BONDS. RX PubMed=26004441; DOI=10.1016/j.str.2015.04.009; RA Bourne Y., Sulzenbacher G., Radic Z., Araoz R., Reynaud M., Benoit E., RA Zakarian A., Servent D., Molgo J., Taylor P., Marchot P.; RT "Marine Macrocyclic Imines, Pinnatoxins A and G: Structural Determinants RT and Functional Properties to Distinguish Neuronal alpha7 from Muscle RT alpha1(2)betagammadelta nAChRs."; RL Structure 23:1106-1115(2015). RN [29] {ECO:0000213|PDB:4ZK4} RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 18-198 AND 215-236, AND DISULFIDE RP BONDS. RA Bobango J., Wu J., Talley T.T.; RT "Crystal structure of a chimeric acetylcholine binding protein from Aplysia RT californica (Ac-AChBP) containing loop C from the human alpha 3 nicotinic RT acetylcholine receptor in complex with 7-(5-isopropoxy-pyridin-3-yl)-1- RT methyl-1,7-diaza-spiro[4.4]nonane."; RL Submitted (APR-2015) to the PDB data bank. RN [30] {ECO:0000213|PDB:5BRX, ECO:0000213|PDB:5BW2} RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 18-236, AND DISULFIDE BONDS. RA Bobango J., Sankaran B., Park J.F., Wu J., Talley T.T.; RT "Comparisons of Binding Affinities for Neuronal Nicotinic Receptors (NNRs) RT and AChBPs."; RL Submitted (JUN-2015) to the PDB data bank. RN [31] {ECO:0000213|PDB:5CO5} RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS), AND DISULFIDE BONDS. RA Wang X.Q., Xu M.Y., Luo S.L., Lin B.; RT "Crystal structure of Ac-AChBP in complex with conotoxin GIC."; RL Submitted (JUL-2015) to the PDB data bank. RN [32] {ECO:0000213|PDB:5LXB} RP X-RAY CRYSTALLOGRAPHY (2.34 ANGSTROMS), AND DISULFIDE BONDS. RX PubMed=27656911; DOI=10.1021/acschemneuro.6b00132; RA Price K.L., Lillestol R.K., Ulens C., Lummis S.C.; RT "Palonosetron-5-HT3 Receptor Interactions As Shown by a Binding Protein RT Cocrystal Structure."; RL ACS Chem. Neurosci. 7:1641-1646(2016). RN [33] {ECO:0000213|PDB:5JME} RP X-RAY CRYSTALLOGRAPHY (2.34 ANGSTROMS) OF 18-236, AND DISULFIDE BONDS. RA Bobango J., McIntosh J.M., Sankaran B., Talley T.T.; RT "Crystal structure of acetylcholine binding protein (AChBP) from Aplysia RT Californica in complex with alpha-conotoxin PeIA."; RL Submitted (APR-2016) to the PDB data bank. RN [34] {ECO:0000213|PDB:5KE4} RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 18-236, AND DISULFIDE BONDS. RA Bobango J., Wu J., Talley I.T., Ralston R., Sankaran B., Talley T.T.; RT "Crystal structure of a chimeric acetylcholine binding protein from Aplysia RT californica (Ac-AChBP) containing loop C from the human alpha 6 nicotinic RT acetylcholine receptor in complex with 2-((5-(3,7-Diazabicyclo[3.3.1]nonan- RT 3-yl)pyridin-3-yl)oxy)-N,N-dimethylethanamine (BPC)."; RL Submitted (JUN-2016) to the PDB data bank. RN [35] {ECO:0000213|PDB:5KZU} RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 18-236, AND DISULFIDE BONDS. RA Bobango J., Wu J., Talley I.T., Sankaran B., Talley T.T.; RT "Crystal structure of a chimeric acetylcholine binding protein from Aplysia RT californica (Ac-AChBP) in complex with click chemistry compound 9-[[1-[8- RT methyl-8-(2-phenylethyl)-8-azoniabicyclo[3.2.1]octan-3-yl]triazol-4- RT yl]methyl]carbazole."; RL Submitted (JUL-2016) to the PDB data bank. RN [36] {ECO:0000213|PDB:5SYO} RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 18-198 AND 215-236, AND DISULFIDE RP BONDS. RA Bobango J., Wu J., Talley I.T., Talley T.T.; RT "Crystal structure of a chimeric acetylcholine binding protein from Aplysia RT californica (Ac-AChBP) containing loop C from the human alpha 3 nicotinic RT acetylcholine receptor in complex with Cytisine."; RL Submitted (AUG-2016) to the PDB data bank. RN [37] {ECO:0000213|PDB:5TVC} RP X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 18-198 AND 215-236, AND DISULFIDE RP BONDS. RA Bobango J., Wu J., Talley I.T., Talley T.T.; RT "Crystal structure of a chimeric acetylcholine binding protein from Aplysia RT californica (Ac-AChBP) containing loop C from the human alpha 3 nicotinic RT acetylcholine receptor in complex with (E,2S)-N-methyl-5-(5-phenoxy-3- RT pyridyl)pent-4-en-2-amine (TI-5312)."; RL Submitted (NOV-2016) to the PDB data bank. RN [38] {ECO:0000213|PDB:5TSF, ECO:0000213|PDB:5TVH} RP X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS) OF 18-236, AND DISULFIDE BONDS. RA Camacho-Hernandez G.A., Kaczanowska K., Harel M., Finn M.G., Taylor P.W.; RT "Crystal structure of AChBP from Aplysia californica complex with 2- RT aminopyrimidine at pH 7.0 spacegroup P212121."; RL Submitted (NOV-2016) to the PDB data bank. RN [39] {ECO:0000213|PDB:5XGL} RP X-RAY CRYSTALLOGRAPHY (3.44 ANGSTROMS) OF 19-236, AND DISULFIDE BONDS. RX PubMed=28585176; DOI=10.1007/s13238-017-0426-2; RA Xu M., Zhu X., Yu J., Yu J., Luo S., Wang X.; RT "The crystal structure of Ac-AChBP in complex with alpha-conotoxin LvIA RT reveals the mechanism of its selectivity towards different nAChR RT subtypes."; RL Protein Cell 8:675-685(2017). RN [40] {ECO:0000213|PDB:5OBH} RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS), AND DISULFIDE BONDS. RA Dawson A., Hunter W.N., Jones M.; RT "Crystal structure of glycine binding protein in complex with RT bicuculline."; RL Submitted (JUN-2017) to the PDB data bank. RN [41] {ECO:0000213|PDB:5O87, ECO:0000213|PDB:5O8T, ECO:0000213|PDB:5OA0} RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS), AND DISULFIDE BONDS. RX PubMed=31709057; DOI=10.1107/S205225251901114X; RA Dawson A., Trumper P., de Souza J.O., Parker H., Jones M.J., Hales T.G., RA Hunter W.N.; RT "Engineering a surrogate human heteromeric alpha/beta glycine receptor RT orthosteric site exploiting the structural homology and stability of RT acetylcholine-binding protein."; RL IUCrJ 6:1014-1023(2019). RN [42] {ECO:0000213|PDB:6QKK} RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS), AND DISULFIDE BONDS. RA Bueno R.V., Davis S., Dawson A., Hunter W.N.; RT "Aplysia californica AChBP in complex with 2-Fluoro- RT (carbamoylpyridinyl)deschloroepibatidine analogue (1)."; RL Submitted (JAN-2019) to the PDB data bank. RN [43] {ECO:0000213|PDB:6QQO, ECO:0000213|PDB:6QQP} RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS), AND DISULFIDE BONDS. RA Bueno R.V., Davis S., Dawson A., Hunter W.N.; RT "Aplysia californica AChBP in complex with 2-Fluoro- RT (carbamoylpyridinyl)deschloroepibatidine analogues."; RL Submitted (FEB-2019) to the PDB data bank. RN [44] {ECO:0000213|PDB:6SH0} RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS), AND DISULFIDE BONDS. RA Hunter W.N., Dawson A., Parker H.; RT "Crystal structure of AcAChBP in complex with anatoxin."; RL Submitted (AUG-2019) to the PDB data bank. RN [45] {ECO:0000213|PDB:6SGV} RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS), AND DISULFIDE BONDS. RA Hunter W.N., Dawson A., Parker H.; RT "Crystal structure of AcAChBP in complex with hosieine."; RL Submitted (AUG-2019) to the PDB data bank. RN [46] {ECO:0000213|PDB:6T9R} RP X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS), AND DISULFIDE BONDS. RX PubMed=32039888; DOI=10.1107/S2053230X20001168; RA Davis S., Rego Campello H., Gallagher T., Hunter W.N.; RT "The thermodynamic profile and molecular interactions of a C(9)-cytisine RT derivative-binding acetylcholine-binding protein from Aplysia RT californica."; RL Acta Crystallogr. F Struct. Biol. Commun. 76:74-80(2020). CC -!- INTERACTION: CC Q8WSF8; Q8WSF8: -; NbExp=8; IntAct=EBI-7179765, EBI-7179765; CC Q8WSF8; P50984; Xeno; NbExp=2; IntAct=EBI-7179765, EBI-15553601; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF322877; AAL37251.1; -; mRNA. DR RefSeq; NP_001191488.1; NM_001204559.1. DR PDB; 2BR7; X-ray; 3.00 A; A/B/C/D/E=20-236. DR PDB; 2BR8; X-ray; 2.40 A; A/B/C/D/E=20-236. DR PDB; 2BYN; X-ray; 2.02 A; A/B/C/D/E=16-236. DR PDB; 2BYP; X-ray; 2.07 A; A/B/C/D/E=18-225. DR PDB; 2BYQ; X-ray; 3.40 A; A/B/C/D/E=16-236. DR PDB; 2BYR; X-ray; 2.45 A; A/B/C/D/E/F/G/H/I/J=18-236. DR PDB; 2BYS; X-ray; 2.05 A; A/B/C/D/E/F/G/H/I/J=16-236. DR PDB; 2C9T; X-ray; 2.25 A; A/B/C/D/E/F/G/H/I/J=20-236. DR PDB; 2PGZ; X-ray; 1.76 A; A/B/C/D/E=18-236. DR PDB; 2PH9; X-ray; 2.88 A; A/B/C/D/E=18-236. DR PDB; 2UZ6; X-ray; 2.40 A; A/B/C/D/E/F/G/H/I/J=20-236. DR PDB; 2W8F; X-ray; 2.70 A; A/B/C/D/E/F/G/H/I/J=20-236. DR PDB; 2W8G; X-ray; 2.60 A; A/B/C/D/E=20-236. DR PDB; 2WN9; X-ray; 1.75 A; A/B/C/D/E=16-236. DR PDB; 2WNC; X-ray; 2.20 A; A/B/C/D/E=18-236. DR PDB; 2WNJ; X-ray; 1.80 A; A/B/C/D/E=16-236. DR PDB; 2WNL; X-ray; 2.70 A; A/B/C/D/E/F/G/H/I/J=16-236. DR PDB; 2WZY; X-ray; 2.51 A; A/B/C/D/E/F/G/H/I/J=16-236. DR PDB; 2X00; X-ray; 2.40 A; A/B/C/E=16-236, D=18-236. DR PDB; 2XNT; X-ray; 3.21 A; A/B/C/D/E/F/G/H/I/J=1-236. DR PDB; 2XNU; X-ray; 2.55 A; A/B/C/D/E=1-236. DR PDB; 2XNV; X-ray; 2.44 A; A/B/C/D/E/F/G/H/I/J=1-236. DR PDB; 2XYS; X-ray; 1.91 A; A/B/C/D/E=20-236. DR PDB; 2XYT; X-ray; 2.05 A; A/B/C/D/E/F/G/H/I/J=20-236. DR PDB; 2XZ5; X-ray; 2.80 A; A/B/C/D/E=20-236. DR PDB; 2XZ6; X-ray; 3.14 A; A/B/C/D/E/F/G/H/I/J=20-236. DR PDB; 2Y54; X-ray; 3.65 A; A/B/C/D/E=20-236. DR PDB; 2Y56; X-ray; 3.59 A; A/B/C/D/E=20-236. DR PDB; 2Y57; X-ray; 3.30 A; A/B/C/D/E=20-236. DR PDB; 2Y58; X-ray; 3.25 A; A/B/C/D/E=20-236. DR PDB; 2Y7Y; X-ray; 1.90 A; A/B/C/D/E=20-236. DR PDB; 2YMD; X-ray; 1.96 A; A/B/C/D/E/F/G/H/I/J=20-231. DR PDB; 2YME; X-ray; 2.40 A; A/B/C/D/E/F/G/H/I/J=20-224. DR PDB; 3C79; X-ray; 2.48 A; A/B/C/D/E=18-236. DR PDB; 3C84; X-ray; 1.94 A; A/B/C/D/E=18-236. DR PDB; 3GUA; X-ray; 3.10 A; A/B/C/D/E/F/G/H/I/J=18-225. DR PDB; 3PEO; X-ray; 2.10 A; A/B/C/D/E/F/G/H/I/J=18-236. DR PDB; 3PMZ; X-ray; 2.44 A; A/B/C/D/E/F/G/H/I/J=18-236. DR PDB; 3SH1; X-ray; 2.90 A; A/B/C/D/E/F/G/H/I/J=18-236. DR PDB; 3SIO; X-ray; 2.32 A; A/B/C/D/E/F/G/H/I/J=18-236. DR PDB; 3T4M; X-ray; 3.00 A; A/B/C/D/E/F/G/H/I/J=18-236. DR PDB; 4AFT; X-ray; 3.20 A; A/B/C/D/E=20-236. DR PDB; 4BFQ; X-ray; 2.40 A; A/B/C/D/E=20-236. DR PDB; 4BQT; X-ray; 2.88 A; A/B/C/D/E=20-236. DR PDB; 4DBM; X-ray; 2.30 A; A/B/C/D/E=18-236. DR PDB; 4EZ1; X-ray; 2.49 A; A/B/C/D/E=18-236. DR PDB; 4FRR; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I/J=18-225. DR PDB; 4WV9; X-ray; 2.00 A; A/B/C/D/E=18-224. DR PDB; 4XHE; X-ray; 1.90 A; A/B/C/D/E/F/G/H/I/J=18-225. DR PDB; 4XK9; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I/J=18-236. DR PDB; 4ZJS; X-ray; 2.23 A; A/B/C/D/E=50-77, A/B/C/D/E=99-236. DR PDB; 4ZK4; X-ray; 1.90 A; A/B/C/D/E=18-71, A/B/C/D/E=73-198, A/B/C/D/E=215-236. DR PDB; 5AIN; X-ray; 2.30 A; A/B/C/D/E=20-231. DR PDB; 5BRX; X-ray; 2.05 A; A/B/C/D/E/F/G/H/I/J=18-236. DR PDB; 5BW2; X-ray; 2.27 A; A/B/C/D/E=18-236. DR PDB; 5CO5; X-ray; 2.10 A; A/B/D/G/I=1-236. DR PDB; 5JME; X-ray; 2.34 A; A/B/C/D/E=18-236. DR PDB; 5KE4; X-ray; 2.55 A; A/B/C/D/E=18-236. DR PDB; 5KZU; X-ray; 2.30 A; A/B/C/D/E=18-236. DR PDB; 5LXB; X-ray; 2.34 A; A/B/C/D/E/F/G/H/I/J=1-236. DR PDB; 5O87; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I/J=1-236. DR PDB; 5O8T; X-ray; 2.20 A; A/B/C/D/E=1-236. DR PDB; 5OA0; X-ray; 2.60 A; A/B/C/D/E=1-236. DR PDB; 5OAD; X-ray; 2.10 A; A/B/C/D/E=1-236. DR PDB; 5OAJ; X-ray; 2.47 A; A/B/C/D/E/F/G/H/I/J=1-236. DR PDB; 5OAL; X-ray; 3.20 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O=1-236. DR PDB; 5OAN; X-ray; 2.60 A; A/B/C/D/E=1-236. DR PDB; 5OBG; X-ray; 2.00 A; A/B/C/D/E=1-236. DR PDB; 5OBH; X-ray; 2.40 A; A/B/C/D/E=1-236. DR PDB; 5SYO; X-ray; 2.00 A; A/B/C/D/E=18-71, A/B/C/D/E=73-198, A/B/C/D/E=215-236. DR PDB; 5TSF; X-ray; 2.29 A; A/B/C/D/E=18-236. DR PDB; 5TVC; X-ray; 1.93 A; A/B/C/D/E=18-71, A/B/C/D/E=73-198, A/B/C/D/E=215-236. DR PDB; 5TVH; X-ray; 2.40 A; A/B/C/D/E=18-236. DR PDB; 5XGL; X-ray; 3.44 A; A/B/D/G/I=19-236. DR PDB; 6QKK; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I/J=1-236. DR PDB; 6QQO; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J=1-236. DR PDB; 6QQP; X-ray; 2.40 A; A/B/C/D/E/F/G/H/I/J=1-236. DR PDB; 6SGV; X-ray; 2.60 A; A/B/C/D/E/F/G/H/I/J=1-236. DR PDB; 6SH0; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J=1-236. DR PDB; 6T9R; X-ray; 1.72 A; AAA/BBB/CCC/DDD/EEE/FFF/GGG/HHH/III/JJJ=1-236. DR PDBsum; 2BR7; -. DR PDBsum; 2BR8; -. DR PDBsum; 2BYN; -. DR PDBsum; 2BYP; -. DR PDBsum; 2BYQ; -. DR PDBsum; 2BYR; -. DR PDBsum; 2BYS; -. DR PDBsum; 2C9T; -. DR PDBsum; 2PGZ; -. DR PDBsum; 2PH9; -. DR PDBsum; 2UZ6; -. DR PDBsum; 2W8F; -. DR PDBsum; 2W8G; -. DR PDBsum; 2WN9; -. DR PDBsum; 2WNC; -. DR PDBsum; 2WNJ; -. DR PDBsum; 2WNL; -. DR PDBsum; 2WZY; -. DR PDBsum; 2X00; -. DR PDBsum; 2XNT; -. DR PDBsum; 2XNU; -. DR PDBsum; 2XNV; -. DR PDBsum; 2XYS; -. DR PDBsum; 2XYT; -. DR PDBsum; 2XZ5; -. DR PDBsum; 2XZ6; -. DR PDBsum; 2Y54; -. DR PDBsum; 2Y56; -. DR PDBsum; 2Y57; -. DR PDBsum; 2Y58; -. DR PDBsum; 2Y7Y; -. DR PDBsum; 2YMD; -. DR PDBsum; 2YME; -. DR PDBsum; 3C79; -. DR PDBsum; 3C84; -. DR PDBsum; 3GUA; -. DR PDBsum; 3PEO; -. DR PDBsum; 3PMZ; -. DR PDBsum; 3SH1; -. DR PDBsum; 3SIO; -. DR PDBsum; 3T4M; -. DR PDBsum; 4AFT; -. DR PDBsum; 4BFQ; -. DR PDBsum; 4BQT; -. DR PDBsum; 4DBM; -. DR PDBsum; 4EZ1; -. DR PDBsum; 4FRR; -. DR PDBsum; 4WV9; -. DR PDBsum; 4XHE; -. DR PDBsum; 4XK9; -. DR PDBsum; 4ZJS; -. DR PDBsum; 4ZK4; -. DR PDBsum; 5AIN; -. DR PDBsum; 5BRX; -. DR PDBsum; 5BW2; -. DR PDBsum; 5CO5; -. DR PDBsum; 5JME; -. DR PDBsum; 5KE4; -. DR PDBsum; 5KZU; -. DR PDBsum; 5LXB; -. DR PDBsum; 5O87; -. DR PDBsum; 5O8T; -. DR PDBsum; 5OA0; -. DR PDBsum; 5OAD; -. DR PDBsum; 5OAJ; -. DR PDBsum; 5OAL; -. DR PDBsum; 5OAN; -. DR PDBsum; 5OBG; -. DR PDBsum; 5OBH; -. DR PDBsum; 5SYO; -. DR PDBsum; 5TSF; -. DR PDBsum; 5TVC; -. DR PDBsum; 5TVH; -. DR PDBsum; 5XGL; -. DR PDBsum; 6QKK; -. DR PDBsum; 6QQO; -. DR PDBsum; 6QQP; -. DR PDBsum; 6T9R; -. DR SMR; Q8WSF8; -. DR DIP; DIP-46103N; -. DR IntAct; Q8WSF8; 2. DR MINT; Q8WSF8; -. DR BindingDB; Q8WSF8; -. DR ChEMBL; CHEMBL1944497; -. DR DrugCentral; Q8WSF8; -. DR GeneID; 100533247; -. DR OrthoDB; 1816421at2759; -. DR EvolutionaryTrace; Q8WSF8; -. DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro. DR GO; GO:0005230; F:extracellular ligand-gated ion channel activity; IEA:InterPro. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro. DR Gene3D; 2.70.170.10; -; 1. DR InterPro; IPR006202; Neur_chan_lig-bd. DR InterPro; IPR036734; Neur_chan_lig-bd_sf. DR InterPro; IPR006201; Neur_channel. DR PANTHER; PTHR18945; PTHR18945; 1. DR Pfam; PF02931; Neur_chan_LBD; 1. DR SUPFAM; SSF63712; SSF63712; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2BR7, ECO:0000213|PDB:2BR8, KW ECO:0000213|PDB:2BYN, ECO:0000213|PDB:2BYP}; KW Magnesium {ECO:0000213|PDB:2WNL, ECO:0000213|PDB:3PMZ, KW ECO:0000213|PDB:3SH1, ECO:0000213|PDB:4ZK4}; KW Metal-binding {ECO:0000213|PDB:2WNL, ECO:0000213|PDB:3PMZ, KW ECO:0000213|PDB:3SH1, ECO:0000213|PDB:4EZ1}; KW Receptor {ECO:0000313|EMBL:AAL37251.1}; Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1..19 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 20..236 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5004316614" FT DOMAIN 34..222 FT /note="Neur_chan_LBD" FT /evidence="ECO:0000259|Pfam:PF02931" FT REGION 153..156 FT /note="Mannose binding" FT /evidence="ECO:0000213|PDB:2PGZ, ECO:0000213|PDB:2WNJ, FT ECO:0000213|PDB:3SIO" FT METAL 42 FT /note="Magnesium 1" FT /evidence="ECO:0000213|PDB:3PMZ" FT METAL 88 FT /note="Magnesium 2" FT /evidence="ECO:0000213|PDB:2WNL" FT METAL 167 FT /note="Magnesium 3" FT /evidence="ECO:0000213|PDB:3PMZ" FT METAL 167 FT /note="Magnesium 4" FT /evidence="ECO:0000213|PDB:3PMZ" FT METAL 170 FT /note="Magnesium 4" FT /evidence="ECO:0000213|PDB:3PMZ" FT METAL 204 FT /note="Magnesium 2; via tele nitrogen" FT /evidence="ECO:0000213|PDB:2WNL" FT BINDING 25 FT /note="Mannose" FT /evidence="ECO:0000213|PDB:2PGZ, ECO:0000213|PDB:2WN9, FT ECO:0000213|PDB:2WNJ" FT BINDING 42 FT /note="Beta-D-mannose; via carbonyl oxygen" FT /evidence="ECO:0000213|PDB:3SIO" FT BINDING 43 FT /note="Mannose" FT /evidence="ECO:0000213|PDB:3SIO" FT BINDING 88 FT /note="Mannose; via carbonyl oxygen" FT /evidence="ECO:0000213|PDB:2PGZ, ECO:0000213|PDB:2WNJ" FT BINDING 179 FT /note="Beta-D-mannose" FT /evidence="ECO:0000213|PDB:3SH1" FT BINDING 197 FT /note="Mannose" FT /evidence="ECO:0000213|PDB:3SIO" FT BINDING 220 FT /note="Beta-D-mannose" FT /evidence="ECO:0000213|PDB:3SIO" FT CARBOHYD 91 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000213|PDB:2BYN, ECO:0000213|PDB:2BYP, FT ECO:0000213|PDB:2PGZ" FT DISULFID 144..157 FT /evidence="ECO:0000213|PDB:2BR7, ECO:0000213|PDB:2BR8, FT ECO:0000213|PDB:2BYN" FT DISULFID 207..208 FT /evidence="ECO:0000213|PDB:2BR7, ECO:0000213|PDB:2BR8, FT ECO:0000213|PDB:2BYN" SQ SEQUENCE 236 AA; 26568 MW; 6D0DE487C46707BE CRC64; MLVSVYLALL VACVGQAHSQ ANLMRLKSDL FNRSPMYPGP TKDDPLTVTL GFTLQDIVKA DSSTNEVDLV YYEQQRWKLN SLMWDPNEYG NITDFRTSAA DIWTPDITAY SSTRPVQVLS PQIAVVTHDG SVMFIPAQRL SFMCDPTGVD SEEGATCAVK FGSWVYSGFE IDLKTDTDQV DLSSYYASSK YEILSATQTR QVQHYSCCPE PYIDVNLVVK FRERRAGNGF FRNLFD //