{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,18]],"date-time":"2026-09-18T21:47:13Z","timestamp":1789768033316,"version":"4.0.1"},"reference-count":27,"publisher":"Wiley","issue":"4","license":[{"start":{"date-parts":[[2008,12,31]],"date-time":"2008-12-31T00:00:00Z","timestamp":1230681600000},"content-version":"vor","delay-in-days":5023,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Protein Science"],"published-print":{"date-parts":[[1995,4]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>The fasciculins are a family of closely related peptides that are isolated from the venom of mambas and exert their toxic action by inhibiting acetylcholinesterase (AChE). Fasciculins belong to the structural family of three\u2010fingered toxins from Elapidae snake venoms, which include the \u03b1\u2010neurotoxins that block the nicotinic acetylcholine receptor and the cardiotoxins that interact with ceil membranes. The features unique to the known primary and tertiary structures of the fasciculin molecule were analyzed. Loop I contains an arginine at position 11, which is found only in the fasciculins and could form a pivotal anchoring point to AChE. Loop II contains five cationic residues near its tip, which are partly charge\u2010compensated by anionic side chains in loop III. By contrast, the other three\u2010fingered toxins show full charge compensation within loop II. The interaction of fasciculin with the recognition site on acetylcholinesterase was investigated by estimating a precollision orientation followed by determination of the buried surface area of the most probable complexes formed, the electrostatic field contours, and the detailed topography of the interaction surface. This approach has led to testable models for the orientation and site of bound fasciculin.<\/jats:p>","DOI":"10.1002\/pro.5560040410","type":"journal-article","created":{"date-parts":[[2010,6,29]],"date-time":"2010-06-29T08:45:16Z","timestamp":1277801116000},"page":"703-715","source":"Crossref","is-referenced-by-count":25,"title":["Theoretical analysis of the structure of the peptide fasciculin and its docking to acetylcholinesterase"],"prefix":"10.1002","volume":"4","author":[{"given":"Harald K. L.","family":"Van Den Born","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zoran","family":"Radi\u0107","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Pascale","family":"Marchot","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Palmer","family":"Taylor","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Igor","family":"Tsigelny","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2008,12,31]]},"reference":[{"key":"e_1_2_1_2_1","doi-asserted-by":"publisher","DOI":"10.1038\/351491a0"},{"key":"e_1_2_1_3_1","first-page":"303","volume-title":"Snake toxins","author":"Cervenansky C","year":"1991"},{"key":"e_1_2_1_4_1","doi-asserted-by":"publisher","DOI":"10.1016\/0304-4165(94)90088-4"},{"key":"e_1_2_1_5_1","doi-asserted-by":"publisher","DOI":"10.1126\/science.6879170"},{"key":"e_1_2_1_6_1","doi-asserted-by":"publisher","DOI":"10.1016\/0163-7258(87)90002-7"},{"key":"e_1_2_1_7_1","first-page":"165","volume-title":"Snake toxins","author":"Endo T","year":"1991"},{"key":"e_1_2_1_8_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi00278a006"},{"key":"e_1_2_1_9_1","doi-asserted-by":"publisher","DOI":"10.1002\/pro.5560030111"},{"key":"e_1_2_1_10_1","first-page":"232","article-title":"Fasciculins, anticholinesterase toxins from the venom of the green mamba Dendroaspis angusticeps","volume":"79","author":"Karlsson E","year":"1984","journal-title":"J Physiol (Paris)"},{"key":"e_1_2_1_11_1","doi-asserted-by":"publisher","DOI":"10.1016\/0163-7258(85)90051-8"},{"key":"e_1_2_1_12_1","doi-asserted-by":"publisher","DOI":"10.1021\/ja00095a050"},{"key":"e_1_2_1_13_1","doi-asserted-by":"crossref","first-page":"22122","DOI":"10.1016\/S0021-9258(18)41644-4","article-title":"1.9\u2010\u00c5 resolution structure of fasciculin 1, an anti\u2010cholinesterase toxin from green mamba snake venom","volume":"267","author":"IeDu MH","year":"1992","journal-title":"J Biol Chem"},{"key":"e_1_2_1_14_1","doi-asserted-by":"publisher","DOI":"10.1093\/protein\/1.1.37"},{"key":"e_1_2_1_15_1","doi-asserted-by":"crossref","first-page":"12458","DOI":"10.1016\/S0021-9258(18)31411-X","article-title":"Binding of 125I\u2010fasciculin to rat brain acetylcholinesterase. 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