{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,18]],"date-time":"2026-08-18T15:30:47Z","timestamp":1787067047274,"version":"build-2736575974"},"reference-count":0,"publisher":"Portland Press Ltd.","issue":"2","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1998,7,15]]},"abstract":"<jats:p>Convulxin (CVX) is a potent platelet-aggregating glycoprotein from the venom of the snake Crotalus durissus terrificus. It consists of two subunits, \u03b1 and \u03b2, joined by disulphide bridges in a hexameric structure. A cDNA library from venom gland was constructed in the vector pT3T7. The cloned cDNAs encoding the two chains of CVX were sequenced. Both are preceded by an identical 23-amino acid peptide signal sequence and encode sequences of 135 amino acids for the \u03b1 chain and 125 amino acids for the \u03b2 chain. These polypeptides include a carbohydrate-recognition domain (CRD) in which some of the specific amino acids required for binding Ca2+ and galactose or mannose are absent. The presence of such a domain means that CVX can be included in the family of C-type lectins along with other snake venom proteins, although it is not a true lectin. Assuming that the localization of intracatenary disulphide bridges of each CVX chain is similar to that of the CRD and that an intercatenary bridge between the \u03b1 and \u03b2 chains is similar to that of the C-type lectin botrocetin, we postulate the existence of an additional intercatenary bridge, which explains the tridimeric structure (\u03b1\u03b2)3 of CVX.<\/jats:p>","DOI":"10.1042\/bj3330389","type":"journal-article","created":{"date-parts":[[2015,8,10]],"date-time":"2015-08-10T18:02:23Z","timestamp":1439229743000},"page":"389-393","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":56,"title":["Cloning of subunits of convulxin, a collagen-like platelet-aggregating protein from Crotalus durissus terrificus venom"],"prefix":"10.1042","volume":"333","author":[{"given":"Mireille","family":"LEDUC","sequence":"first","affiliation":[{"name":"Unit\u00e9 des Venins, Institut Pasteur, 25 Rue du Dr. Roux, 75724 Paris Cedex 15, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Cassian","family":"BON","sequence":"additional","affiliation":[{"name":"Unit\u00e9 des Venins, Institut Pasteur, 25 Rue du Dr. Roux, 75724 Paris Cedex 15, France"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/333\/2\/389\/631343\/bj3330389.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/333\/2\/389\/631343\/bj3330389.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,23]],"date-time":"2021-11-23T19:33:58Z","timestamp":1637696038000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/333\/2\/389\/34054\/Cloning-of-subunits-of-convulxin-a-collagen-like"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1998,7,15]]},"references-count":0,"journal-issue":{"issue":"2","published-print":{"date-parts":[[1998,7,15]]}},"URL":"https:\/\/doi.org\/10.1042\/bj3330389","relation":{},"ISSN":["0264-6021","1470-8728"],"issn-type":[{"value":"0264-6021","type":"print"},{"value":"1470-8728","type":"electronic"}],"subject":[],"published":{"date-parts":[[1998,7,15]]}}}