{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T16:35:37Z","timestamp":1791218137383,"version":"4.1.0"},"reference-count":37,"publisher":"National Academy of Sciences","issue":"13","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2010,3,30]]},"abstract":"<jats:p>\n                    Spirolide and gymnodimine macrocyclic imine phycotoxins belong to an emerging class of chemical agents associated with marine algal blooms and shellfish toxicity. Analysis of 13-desmethyl spirolide C and gymnodimine A by binding and voltage-clamp recordings on muscle-type \u03b11\n                    <jats:sub>2<\/jats:sub>\n                    \u03b2\u03b3\u03b4 and neuronal \u03b13\u03b22 and \u03b14\u03b22 nicotinic acetylcholine receptors reveals subnanomolar affinities, potent antagonism, and limited subtype selectivity. Their binding to acetylcholine-binding proteins (AChBP), as soluble receptor surrogates, exhibits picomolar affinities governed by diffusion-limited association and slow dissociation, accounting for apparent irreversibility. Crystal structures of the phycotoxins bound to\n                    <jats:italic>Aplysia<\/jats:italic>\n                    -AChBP (\u22482.4\u00c5) show toxins neatly imbedded within the nest of ar-omatic side chains contributed by loops C and F on opposing faces of the subunit interface, and which in physiological conditions accommodates acetylcholine. The structures also point to three major features: (\n                    <jats:italic>i<\/jats:italic>\n                    ) the sequence-conserved loop C envelops the bound toxins to maximize surface complementarity; (\n                    <jats:italic>ii<\/jats:italic>\n                    ) hydrogen bonding of the protonated imine nitrogen in the toxins with the carbonyl oxygen of loop C Trp147 tethers the toxin core centered within the pocket; and (\n                    <jats:italic>iii<\/jats:italic>\n                    ) the spirolide\n                    <jats:italic>bis<\/jats:italic>\n                    -spiroacetal or gymnodimine tetrahydrofuran and their common cyclohexene-butyrolactone further anchor the toxins in apical and membrane directions, along the subunit interface. In contrast, the se-quence-variable loop F only sparingly contributes contact points to preserve the broad receptor subtype recognition unique to phycotoxins compared with other nicotinic antagonists. These data offer unique means for detecting spiroimine toxins in shellfish and identify distinctive ligands, functional determinants and binding regions for the design of new drugs able to target several receptor subtypes with high affinity.\n                  <\/jats:p>","DOI":"10.1073\/pnas.0912372107","type":"journal-article","created":{"date-parts":[[2010,3,11]],"date-time":"2010-03-11T22:14:04Z","timestamp":1268345644000},"page":"6076-6081","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":147,"title":["Structural determinants in phycotoxins and AChBP conferring high affinity binding and nicotinic AChR antagonism"],"prefix":"10.1073","volume":"107","author":[{"given":"Yves","family":"Bourne","sequence":"first","affiliation":[{"name":"Architecture et Fonction des Macromol\u00e9cules Biologiques, Centre National de la Recherche Scientifique, Universit\u00e9 d\u2019Aix-Marseille, Campus Luminy\u2013Case 932, F-13288 Marseille Cedex 9, France;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zoran","family":"Radi\u0107","sequence":"additional","affiliation":[{"name":"Department of Pharmacology, Skaggs School of Pharmacy and Pharmaceutical Sciences, University of California at San Diego, La Jolla, CA 92093-0657;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"R\u00f3mulo","family":"Ar\u00e1oz","sequence":"additional","affiliation":[{"name":"Laboratoire de Neurobiologie Cellulaire et Mol\u00e9culaire, Centre National de la Recherche Scientifique, Institut de Neurobiologie Alfred Fessard\u2013FRC2118, F-91198 Gif-sur-Yvette Cedex, France;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Todd T.","family":"Talley","sequence":"additional","affiliation":[{"name":"Department of Pharmacology, Skaggs School of Pharmacy and Pharmaceutical Sciences, University of California at San Diego, La Jolla, CA 92093-0657;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Evelyne","family":"Benoit","sequence":"additional","affiliation":[{"name":"Laboratoire de Neurobiologie Cellulaire et Mol\u00e9culaire, Centre National de la Recherche Scientifique, Institut de Neurobiologie Alfred Fessard\u2013FRC2118, F-91198 Gif-sur-Yvette Cedex, France;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Denis","family":"Servent","sequence":"additional","affiliation":[{"name":"Institut de Biologie et Technologies de Saclay, Service d'Ing\u00e9nierie Mol\u00e9culaire des Prot\u00e9ines, Laboratoire de Toxinologie Mol\u00e9culaire, Commissariat \u00e0 l'Energie Atomique, F-91191 Gif-sur-Yvette, France; and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Palmer","family":"Taylor","sequence":"additional","affiliation":[{"name":"Department of Pharmacology, Skaggs School of Pharmacy and Pharmaceutical Sciences, University of California at San Diego, La Jolla, CA 92093-0657;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jordi","family":"Molg\u00f3","sequence":"additional","affiliation":[{"name":"Laboratoire de Neurobiologie Cellulaire et Mol\u00e9culaire, Centre National de la Recherche Scientifique, Institut de Neurobiologie Alfred Fessard\u2013FRC2118, F-91198 Gif-sur-Yvette Cedex, France;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Pascale","family":"Marchot","sequence":"additional","affiliation":[{"name":"Centre de Recherche en Neurobiologie-Neurophysiologie de Marseille, Centre National de la Recherche Scientifique, Universit\u00e9 d\u2019Aix-Marseille, Institut F\u00e9d\u00e9ratif de Recherche Jean Roche, Facult\u00e9 de M\u00e9decine\u2013Secteur Nord, CS80011, F-13344 Marseille Cedex 15, France"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[2010,3,11]]},"reference":[{"key":"e_1_3_4_1_2","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1007\/978-3-540-30880-5_3","article-title":"Bivalve molluscs as vectors of marine biotoxins involved in seafood poisoning","volume":"43","author":"Ciminiello P","year":"2006","unstructured":"P Ciminiello, E Fattorusso, Bivalve molluscs as vectors of marine biotoxins involved in seafood poisoning. 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J Nat Prod 69, 983\u2013987 (2006).","journal-title":"J Nat Prod"},{"key":"e_1_3_4_9_2","doi-asserted-by":"crossref","first-page":"1878","DOI":"10.1021\/np0703242","article-title":"Spirolide toxin profile of Adriatic Alexandrium ostenfeldii cultures and structure elucidation of 27-hydroxy-13,19-didesmethyl spirolide C","volume":"70","author":"Ciminiello P","year":"2007","unstructured":"P Ciminiello, et al., Spirolide toxin profile of Adriatic Alexandrium ostenfeldii cultures and structure elucidation of 27-hydroxy-13,19-didesmethyl spirolide C. J Nat Prod 70, 1878\u20131883 (2007).","journal-title":"J Nat Prod"},{"key":"e_1_3_4_10_2","doi-asserted-by":"crossref","first-page":"319","DOI":"10.1002\/9780470277874.ch18","volume-title":"Phycotoxins: Chemistry and Biochemistry","author":"Molg\u00f3 J","year":"2007","unstructured":"J Molg\u00f3, E Girard, E Benoit, The cyclic imines: An insight into this emerging group of bioactive marine toxins. 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Tetrahedron Lett 36, 7093\u20137096 (1995).","journal-title":"Tetrahedron Lett"},{"key":"e_1_3_4_13_2","doi-asserted-by":"crossref","first-page":"1373","DOI":"10.1021\/jf991031k","article-title":"New analogue of gymnodimine from a Gymnodinium species","volume":"48","author":"Miles CO","year":"2000","unstructured":"CO Miles, AL Wilkins, DJ Stirling, AL MacKenzie, New analogue of gymnodimine from a Gymnodinium species. J Agric Food Chem 48, 1373\u20131376 (2000).","journal-title":"J Agric Food Chem"},{"key":"e_1_3_4_14_2","doi-asserted-by":"crossref","first-page":"4838","DOI":"10.1021\/jf030101r","article-title":"Gymnodimine C, an isomer of gymnodimine B, from Karenia selliformis","volume":"51","author":"Miles CO","year":"2003","unstructured":"CO Miles, AL Wilkins, DJ Stirling, AL MacKenzie, Gymnodimine C, an isomer of gymnodimine B, from Karenia selliformis. J Agric Food Chem 51, 4838\u20134840 (2003).","journal-title":"J Agric Food Chem"},{"key":"e_1_3_4_15_2","doi-asserted-by":"crossref","first-page":"952","DOI":"10.1111\/j.1471-4159.2008.05677.x","article-title":"The marine phycotoxin gymnodimine targets muscular and neuronal nicotinic acetylcholine receptor subtypes with high affinity","volume":"107","author":"Kharrat R","year":"2008","unstructured":"R Kharrat, et al., The marine phycotoxin gymnodimine targets muscular and neuronal nicotinic acetylcholine receptor subtypes with high affinity. J Neurochem 107, 952\u2013963 (2008).","journal-title":"J Neurochem"},{"key":"e_1_3_4_16_2","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1016\/j.toxicon.2004.05.017","article-title":"Acute toxicity of gymnodimine to mice","volume":"44","author":"Munday R","year":"2004","unstructured":"R Munday, et al., Acute toxicity of gymnodimine to mice. Toxicon 44, 173\u2013178 (2004).","journal-title":"Toxicon"},{"key":"e_1_3_4_17_2","doi-asserted-by":"crossref","first-page":"1424","DOI":"10.1126\/science.1108595","article-title":"Allosteric mechanisms of signal transduction","volume":"308","author":"Changeux JP","year":"2005","unstructured":"JP Changeux, SJ Edelstein, Allosteric mechanisms of signal transduction. Science 308, 1424\u20131428 (2005).","journal-title":"Science"},{"key":"e_1_3_4_18_2","first-page":"217","volume-title":"Goodman and Gilman's The Pharmacological Basis of Therapeutics","author":"Taylor P","year":"2006","unstructured":"P Taylor, Agents acting at the neuromuscular junction and autonomic ganglia. Goodman and Gilman's The Pharmacological Basis of Therapeutics, eds LL Brunton, JS Lazo, KL Parker (McGraw\u2013Hill , New York), pp. 217\u2013236 (2006)."},{"key":"e_1_3_4_19_2","doi-asserted-by":"crossref","first-page":"447","DOI":"10.1002\/neu.10153","article-title":"The diversity of subunit composition in nAChRs: Evolutionary origins, physiologic and pharmacologic consequences","volume":"53","author":"Le Nov\u00e8re N","year":"2002","unstructured":"N Le Nov\u00e8re, PJ Corringer, JP Changeux, The diversity of subunit composition in nAChRs: Evolutionary origins, physiologic and pharmacologic consequences. J Neurobiol 53, 447\u2013456 (2002).","journal-title":"J Neurobiol"},{"key":"e_1_3_4_20_2","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1038\/35077011","article-title":"Crystal structure of an ACh-binding protein reveals the ligand-binding domain of nicotinic receptors","volume":"411","author":"Brejc K","year":"2001","unstructured":"K Brejc, et al., Crystal structure of an ACh-binding protein reveals the ligand-binding domain of nicotinic receptors. Nature 411, 269\u2013276 (2001).","journal-title":"Nature"},{"key":"e_1_3_4_21_2","doi-asserted-by":"crossref","first-page":"907","DOI":"10.1016\/S0896-6273(04)00115-1","article-title":"Nicotine and carbamylcholine binding to nicotinic acetylcholine receptors as studied in AChBP crystal structures","volume":"41","author":"Celie PH","year":"2004","unstructured":"PH Celie, et al., Nicotine and carbamylcholine binding to nicotinic acetylcholine receptors as studied in AChBP crystal structures. Neuron 41, 907\u2013914 (2004).","journal-title":"Neuron"},{"key":"e_1_3_4_22_2","doi-asserted-by":"crossref","first-page":"41299","DOI":"10.1074\/jbc.C200462200","article-title":"Tryptophan fluorescence reveals conformational changes in the acetylcholine binding protein","volume":"277","author":"Hansen SB","year":"2002","unstructured":"SB Hansen, et al., Tryptophan fluorescence reveals conformational changes in the acetylcholine binding protein. J Biol Chem 277, 41299\u201341302 (2002).","journal-title":"J Biol Chem"},{"key":"e_1_3_4_23_2","doi-asserted-by":"crossref","first-page":"1512","DOI":"10.1038\/sj.emboj.7600620","article-title":"Crystal structure of a Cbtx-AChBP complex reveals essential interactions between snake \u03b1-neurotoxins and nicotinic receptors","volume":"24","author":"Bourne Y","year":"2005","unstructured":"Y Bourne, TT Talley, SB Hansen, P Taylor, P Marchot, Crystal structure of a Cbtx-AChBP complex reveals essential interactions between snake \u03b1-neurotoxins and nicotinic receptors. EMBO J 24, 1512\u20131522 (2005).","journal-title":"EMBO J"},{"key":"e_1_3_4_24_2","doi-asserted-by":"crossref","first-page":"3635","DOI":"10.1038\/sj.emboj.7600828","article-title":"Structures of Aplysia AChBP complexes with nicotinic agonists and antagonists reveal distinctive binding interfaces and conformations","volume":"24","author":"Hansen SB","year":"2005","unstructured":"SB Hansen, et al., Structures of Aplysia AChBP complexes with nicotinic agonists and antagonists reveal distinctive binding interfaces and conformations. EMBO J 24, 3635\u20133646 (2005).","journal-title":"EMBO J"},{"key":"e_1_3_4_25_2","doi-asserted-by":"crossref","first-page":"3040","DOI":"10.1038\/emboj.2009.227","article-title":"Structural determinants for interaction of partial agonists with acetylcholine binding protein and neuronal alpha7 nicotinic acetylcholine receptor","volume":"28","author":"Hibbs RE","year":"2009","unstructured":"RE Hibbs, et al., Structural determinants for interaction of partial agonists with acetylcholine binding protein and neuronal alpha7 nicotinic acetylcholine receptor. EMBO J 28, 3040\u20133051 (2009).","journal-title":"EMBO J"},{"key":"e_1_3_4_26_2","doi-asserted-by":"crossref","first-page":"6692","DOI":"10.1016\/S0021-9258(19)69047-2","article-title":"Relationship between reversible antagonist occupancy and the functional capacity of the acetylcholine receptor","volume":"256","author":"Sine SM","year":"1981","unstructured":"SM Sine, P Taylor, Relationship between reversible antagonist occupancy and the functional capacity of the acetylcholine receptor. J Biol Chem 256, 6692\u20136699 (1981).","journal-title":"J Biol Chem"},{"key":"e_1_3_4_27_2","doi-asserted-by":"crossref","first-page":"24197","DOI":"10.1074\/jbc.M402452200","article-title":"Structural and ligand recognition characteristics of an acetylcholine-binding protein from Aplysia californica","volume":"279","author":"Hansen SB","year":"2004","unstructured":"SB Hansen, TT Talley, Z Radi\u0107, P Taylor, Structural and ligand recognition characteristics of an acetylcholine-binding protein from Aplysia californica. J Biol Chem 279, 24197\u201324202 (2004).","journal-title":"J Biol Chem"},{"key":"e_1_3_4_28_2","doi-asserted-by":"crossref","first-page":"8659","DOI":"10.1016\/S0040-4020(01)00861-4","article-title":"Assignment of the relative stereochemistry of the spirolides, macrocyclic toxins isolated from shellfish and from the cultured dinoflagellate Alexandrium ostenfeldii","volume":"57","author":"Falk M","year":"2001","unstructured":"M Falk, IW Burton, T Hu, JA Walter, JLC Wright, Assignment of the relative stereochemistry of the spirolides, macrocyclic toxins isolated from shellfish and from the cultured dinoflagellate Alexandrium ostenfeldii. Tetrahedron 57, 8659\u20138665 (2001).","journal-title":"Tetrahedron"},{"key":"e_1_3_4_29_2","doi-asserted-by":"crossref","first-page":"255","DOI":"10.3390\/md403255","article-title":"The nemertine toxin anabaseine and its derivative DMXBA (GTS-21): Chemical and pharmacological properties","volume":"4","author":"Kem W","year":"2006","unstructured":"W Kem, et al., The nemertine toxin anabaseine and its derivative DMXBA (GTS-21): Chemical and pharmacological properties. Mar Drugs 4, 255\u2013273 (2006).","journal-title":"Mar Drugs"},{"key":"e_1_3_4_30_2","first-page":"8894","article-title":"Spectroscopic analysis of benzylidene anabaseine complexes with acetylcholine binding proteins as models for ligand-nicotinic receptor interactions","volume":"45","author":"Talley TT","year":"2006","unstructured":"TT Talley, et al., Spectroscopic analysis of benzylidene anabaseine complexes with acetylcholine binding proteins as models for ligand-nicotinic receptor interactions. Bio-chemistry 45, 8894\u20138902 (2006).","journal-title":"Bio-chemistry"},{"key":"e_1_3_4_31_2","first-page":"253","article-title":"Characterization of cembranoid interaction with the nicotinic acetylcholine receptor","volume":"287","author":"Hann RM","year":"1998","unstructured":"RM Hann, et al., Characterization of cembranoid interaction with the nicotinic acetylcholine receptor. J Pharmacol Exp Ther 287, 253\u2013260 (1998).","journal-title":"J Pharmacol Exp Ther"},{"key":"e_1_3_4_32_2","doi-asserted-by":"crossref","first-page":"1798","DOI":"10.1021\/jm00110a007","article-title":"Structure\/activity and molecular modeling studies of the lophotoxin family of irreversible nicotinic receptor antagonists","volume":"34","author":"Abramson SN","year":"1991","unstructured":"SN Abramson, et al., Structure\/activity and molecular modeling studies of the lophotoxin family of irreversible nicotinic receptor antagonists. J Med Chem 34, 1798\u20131804 (1991).","journal-title":"J Med Chem"},{"key":"e_1_3_4_33_2","doi-asserted-by":"crossref","first-page":"281","DOI":"10.1074\/jbc.270.1.281","article-title":"Lophotoxin is a slow binding irreversible inhibitor of nicotinic acetylcholine receptors","volume":"270","author":"Groebe DR","year":"1995","unstructured":"DR Groebe, SN Abramson, Lophotoxin is a slow binding irreversible inhibitor of nicotinic acetylcholine receptors. J Biol Chem 270, 281\u2013286 (1995).","journal-title":"J Biol Chem"},{"key":"e_1_3_4_34_2","doi-asserted-by":"crossref","first-page":"5579","DOI":"10.1021\/bi00236a034","article-title":"Serine-specific phosphorylation of nicotinic receptor associated 43K protein","volume":"30","author":"Hill JA","year":"1991","unstructured":"JA Hill, HO Nghi\u00eam, JP Changeux, Serine-specific phosphorylation of nicotinic receptor associated 43K protein. Biochemistry 30, 5579\u20135585 (1991).","journal-title":"Biochemistry"},{"key":"e_1_3_4_35_2","doi-asserted-by":"crossref","first-page":"24279","DOI":"10.1074\/jbc.272.39.24279","article-title":"Only snake curaremimetic toxins with a fifth disulfide bond have high affinity for the neuronal \u03b17 nicotinic receptor","volume":"272","author":"Servent D","year":"1997","unstructured":"D Servent, et al., Only snake curaremimetic toxins with a fifth disulfide bond have high affinity for the neuronal \u03b17 nicotinic receptor. J Biol Chem 272, 24279\u201324286 (1997).","journal-title":"J Biol Chem"},{"key":"e_1_3_4_36_2","doi-asserted-by":"crossref","first-page":"1146","DOI":"10.1002\/cbic.200700757","article-title":"Fluorescent agonists for the Torpedo nicotinic acetylcholine receptor","volume":"9","author":"Krieger F","year":"2008","unstructured":"F Krieger, et al., Fluorescent agonists for the Torpedo nicotinic acetylcholine receptor. 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