C-type lectin-like proteins from snake venoms

Abstract

C-type lectin-like proteins (CTLs) as found in snake venoms fulfill various physiological functions. They play a role in hemostasis and have helped elucidate mechanisms involved in blood coagulation and platelet activation. Their basic structure consists of the subunits α and β, which form heterodimers via a typical domain-swapping motif. These heterodimers can form oligomers such as the tetrameric flavocetin-A and convulxin, which arrange into cyclic structures. Rhodocetin is a selective α2β1 integrin antagonist consisting of four distinct subunits forming a novel cruciform structure. Along with EMS16 and VP12, rhodocetin inhibits collagen-binding to the α2A-domain. These integrin-specific antagonists are lead structures for the development of antimetastatic and antiangiogenic drugs.