The disulfide bridge pattern of snake venom disintegrins, flavoridin and echistatin
- 14 September 1992
- journal article
- Published by Wiley in FEBS Letters
- Vol. 309 (3), 316-320
- https://doi.org/10.1016/0014-5793(92)80797-k
Abstract
Flavoridin and echistatin, isolated from the venom of Trimeresurus flavoviridis and Echis carinatus, respectively, belong to the disintegrin family of integrin β1 and β3 inhibitors of low molecular weight RGD-containing, cysteine-rich peptides. Since disulfide bonds are critical for expression of biological activity, we sought to determine their location in these two proteins. In flavoridin, direct evidence for the existence of linkage between Cys4-Cys10 and between Cys45 and Cys64 was obtained by analysis of proteolytic products, and indirect evidence suggests links between Cys13-Cys14 and Cys13-Cys14. In echistatin, links between Cys14-Cys37 and Cys20-Cys34 were identified by direct chemical analysis.Keywords
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