{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,11]],"date-time":"2026-02-11T13:13:32Z","timestamp":1770815612290,"version":"3.50.1"},"reference-count":72,"publisher":"Portland Press Ltd.","issue":"8","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2019,4,30]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>\u03b1\u03b4-Bungarotoxins, a novel group of long-chain \u03b1-neurotoxins, manifest different affinity to two agonist\/competitive antagonist binding sites of muscle-type nicotinic acetylcholine receptors (nAChRs), being more active at the interface of \u03b1\u2013\u03b4 subunits. Three isoforms (\u03b1\u03b4-BgTx-1\u20133) were identified in Malayan Krait (Bungarus candidus) from Thailand by genomic DNA analysis; two of them (\u03b1\u03b4-BgTx-1 and 2) were isolated from its venom. The toxins comprise 73 amino acid residues and 5 disulfide bridges, being homologous to \u03b1-bungarotoxin (\u03b1-BgTx), a classical blocker of muscle-type and neuronal \u03b17, \u03b18, and \u03b19\u03b110 nAChRs. The toxicity of \u03b1\u03b4-BgTx-1 (LD50\u2009=\u20090.17\u20130.28\u2005\u00b5g\/g mouse, i.p. injection) is essentially as high as that of \u03b1-BgTx. In the chick biventer cervicis nerve\u2013muscle preparation, \u03b1\u03b4-BgTx-1 completely abolished acetylcholine response, but in contrast with the block by \u03b1-BgTx, acetylcholine response was fully reversible by washing. \u03b1\u03b4-BgTxs, similar to \u03b1-BgTx, bind with high affinity to \u03b17 and muscle-type nAChRs. However, the major difference of \u03b1\u03b4-BgTxs from \u03b1-BgTx and other naturally occurring \u03b1-neurotoxins is that \u03b1\u03b4-BgTxs discriminate the two binding sites in the Torpedo californica and mouse muscle nAChRs showing up to two orders of magnitude higher affinity for the \u03b1\u2013\u03b4 site as compared with \u03b1\u2013\u03b5 or \u03b1\u2013\u03b3 binding site interfaces. Molecular modeling and analysis of the literature provided possible explanations for these differences in binding mode; one of the probable reasons being the lower content of positively charged residues in \u03b1\u03b4-BgTxs. Thus, \u03b1\u03b4-BgTxs are new tools for studies on nAChRs.<\/jats:p>","DOI":"10.1042\/bcj20180909","type":"journal-article","created":{"date-parts":[[2019,4,3]],"date-time":"2019-04-03T21:59:29Z","timestamp":1554328769000},"page":"1285-1302","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":24,"title":["Novel long-chain neurotoxins from <i>Bungarus candidus<\/i> distinguish the two binding sites in muscle-type nicotinic acetylcholine receptors"],"prefix":"10.1042","volume":"476","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-4609-970X","authenticated-orcid":false,"given":"Yuri N.","family":"Utkin","sequence":"first","affiliation":[{"name":"Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia"},{"name":"The National University of Science and Technology MISIS, Moscow, 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