Disintegrin

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Structure of disintegrin heterodimer from Echis carinatus.
Structure of disintegrin heterodimer from Echis carinatus.

Disintegrins are peptides isolated from the venom of various snakes of the viper family. They interact with the beta 1 and beta 3 families of integrin proteins. Disintegrins are cysteine-rich peptides ranging from 45 to 84 amino acids in length and almost all of them contain an Arg-Gly-Asp (RGD) sequence, a recognition site of many adhesion proteins.

They work by countering the blood clotting steps, inhibiting the clumping of platelets.

Examples of disintegrins are: albolabrin, applagin, barbourin, batroxostatin, bitistatin, echistatin, elegantin, eristicophin, flavoridin, halysin, kistrin, tergeminin and triflavin.

The term disintegrin was first proposed by R. J. Gould et al. in 1989.

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