The disulfide bridge pattern of snake venom disintegrins, flavoridin and echistatin

descriptionPublicationkeyboard_double_arrow_right Article 14 Sep 1992 English Publisher:WileyJournal:FEBS Letters, volume 309, pages 316-320 (issn: 0014-5793, eissn: 1873-3468,

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Authors: Calvete, Juan J.; Wang, Yuqin; Mann, Karlheinz; Schäfer, Wolfram; Niewiarowski, Stefan; Stewart, Gwendolyn J.;

doi: 10.1016/0014-5793(92)80797-k

pmid: 1516704

handle: 10261/256190

The disulfide bridge pattern of snake venom disintegrins, flavoridin and echistatin

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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.

Related Organizations

Temple University
United States
Spanish National Research Council
Spain
Max Planck Institute of Biochemistry
Germany
Max Planck Society
Germany

Keywords

Integrins, Inhibitor of integrin: Disintegrin, Flavoridin, Disullfide bridge, Disintegrin, Molecular Sequence Data, Viper Venoms, Echistatin, Crotalid Venoms, Intercellular Signaling Peptides and Proteins, Disulfide bridge, Amino Acid Sequence, Cysteine, Disulfides, Peptides, Inhibitor of integrin

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