{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,3]],"date-time":"2026-10-03T19:09:49Z","timestamp":1791054589301,"version":"4.1.0"},"reference-count":44,"publisher":"Wiley","issue":"4","license":[{"start":{"date-parts":[[2004,8,18]],"date-time":"2004-08-18T00:00:00Z","timestamp":1092787200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Proteins"],"published-print":{"date-parts":[[2004,12]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>\u03b3\u2010Bungarotoxin, a snake venom protein isolated from <jats:italic>Bungarus multicinctus<\/jats:italic>, contains 68 amino acids, including 10 cysteine residues and a TAVRGDGP sequence at positions 30\u201337. The solution structure of \u03b3\u2010bungarotoxin has been determined by nuclear magnetic resonance (NMR) spectroscopy. The structure is similar to that of the short\u2010chain neurotoxins that contain three loops extending from a disulfide\u2010bridged core. The tripeptide Arg\u2010Gly\u2010Asp (RGD) sequence is located at the apex of the flexible loop and is similar to that of other RGD\u2010containing proteins. However, \u03b3\u2010bungarotoxin only inhibits platelet aggregations with an IC50 of 34 \u03bcM. To understand its weak activity in inhibiting platelet aggregation, we mutated the RGD loop sequences of rhodostomin, a potent platelet aggregation inhibitor, from RIPRGDMP to TAVRGDGP, resulting in a 196\u2010fold decrease in activity. In addition, the average C\u03b1\u2010to\u2010C\u03b1 distance between R33 and G36 of \u03b3\u2010bungarotoxin is 6.02 \u00c5, i.e., shorter than that of other RGD\u2010containing proteins that range from 6.55 to 7.46 \u00c5. These results suggested that the amino acid residues flanking the RGD motif might control the width of the RGD loop. This structural difference may be responsible for its decrease in platelet aggregation inhibition compared with other RGD\u2010containing proteins. Proteins 2004. \u00a9 2004 Wiley\u2010Liss, Inc.<\/jats:p>","DOI":"10.1002\/prot.20269","type":"journal-article","created":{"date-parts":[[2004,8,19]],"date-time":"2004-08-19T16:44:27Z","timestamp":1092933867000},"page":"839-849","source":"Crossref","is-referenced-by-count":37,"title":["Solution structure of \u03b3\u2010bungarotoxin: The functional significance of amino acid residues flanking the RGD motif in integrin 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