The disulfide bridge pattern of snake venom disintegrins, flavoridin and echistatin.
Flavoridin and echistatin, isolated from the venom of Trimeresurus flavoviridis and Echis carinatus, respectively, belong to the disintegrin family of integrin beta 1 and beta 3 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-Cys19 and between Cys45 and Cys64 was obtained by analysis of proteolytic products, and indirect evidence suggests links between Cys6-Cys14 and Cys13-Cys36. In echistatin, links between Cys8-Cys37 and Cys20-Cys39 were identified by direct chemical analysis.
Calvete
J J
JJ
Max-Planck-Institut für Biochemie, Martinsried, Germany.
Wang
Y
Y
Mann
K
K
Schäfer
W
W
Niewiarowski
S
S
Stewart
G J
GJ
D000595:Amino Acid Sequence; D003435:Crotalid Venoms / Q000737:chemistry*; D003545:Cysteine / Q000737:chemistry; D004220:Disulfides / Q000032:analysis*; D016023:Integrins / Q000037:antagonists & inhibitors*; D036341:Intercellular Signaling Peptides and Proteins; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D014757:Viper Venoms / Q000737:chemistry*
D003435:Crotalid Venoms; D004220:Disulfides; D016023:Integrins; D036341:Intercellular Signaling Peptides and Proteins; D010455:Peptides; D014757:Viper Venoms; C057986:echistatin; C069044:flavoridin protein, Trimeresurus; D003545:Cysteine