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PMID: 2236100 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S. Review

Disintegrins: a family of integrin inhibitory proteins from viper venoms.

Gould RJ, Polokoff MA, Friedman PA, Huang TF, Holt JC, Cook JJ, Niewiarowski S

Abstract

Disintegrins represent a new class of low molecular weight, RGD-containing, cysteine-rich peptides isolated from the venom of various snakes. They interact with the beta 1 and beta 3 families of integrins and their potency is at least 500-2000 times higher than short RGDX peptides. Analysis of the amino acid sequences of 14 different disintegrins suggests that the RGD sequence, in the spatial configuration determined by the appropriate pairing of the cysteine residues, functions as a cell recognition site. However, certain nonconserved amino acids appear to modify the activity of disintegrins, their specificity for various receptors, and their ability to compete specifically with various ligands.

MeSH Terms
Amino Acid Sequence Animals Humans Integrins/antagonists & inhibitors Molecular Sequence Data Oligopeptides/analysis Viper Venoms/analysis
Chemicals
Integrins Oligopeptides Viper Venoms arginyl-glycyl-aspartic acid
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Gould R J
Department of Biological Chemistry, Merck, Sharp & Dohme Research Laboratories, West Point, Pennsylvania 19486.
Polokoff M A
Friedman P A
Huang T F
Holt J C
Cook J J
Niewiarowski S
Article Info
Journal
Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine (New York, N.Y.)
Abbr.
Proc Soc Exp Biol Med
ISSN
0037-9727
Published
1990-11-00
Pages
168-71
Language
English
Region
United States
NLM ID
7505892
Subset
IM
Grants
FIC NIH HHS · F05TW03682 · United States
NHLBI NIH HHS · HL15226 · United States
NHLBI NIH HHS · HL36579 · United States
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