Structure-function correlations of snake venom disintegrins.
Disintegrins represent a family of polypeptides released in the venoms of Viperidae and Crotalidae snakes (vipers and rattlesnakes) by the proteolytic processing of multidomain metalloproteinases, which selectively block the function of beta(1) and beta(3) integrin receptors. Research on disintegrins is relevant for understanding the biology of viper venom toxins, but also provides information of new structural determinants involved in integrin recognition that may be useful in both, basic and clinical research. The role of the composition, conformation and concerted dynamics of the integrin inhibitory loop and the C-terminal tail in determining the selective inhibition of integrin receptors is discussed.
Calvete
Juan J
JJ
Instituto de Biomedicina de Valencia, C.S.I.C., Valencia, Spain. jcalvete@ibv.csic.es
D000595:Amino Acid Sequence; D000818:Animals; D003435:Crotalid Venoms / Q000737:chemistry; D019483:Disintegrins / Q000737:chemistry* / Q000494:pharmacology*; D006801:Humans; D016023:Integrins / Q000037:antagonists & inhibitors / Q000737:chemistry; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010975:Platelet Aggregation Inhibitors / Q000737:chemistry* / Q000494:pharmacology*; D012910:Snake Venoms / Q000737:chemistry*; D013329:Structure-Activity Relationship; D014757:Viper Venoms / Q000737:chemistry
D003435:Crotalid Venoms; D019483:Disintegrins; D016023:Integrins; D010975:Platelet Aggregation Inhibitors; D012910:Snake Venoms; D014757:Viper Venoms