C-type lectin-like proteins from snake venoms.
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.
Center for Molecular Medicine, Department of Vascular Matrix Biology, Excellence Cluster Cardio-Pulmonary System, Frankfurt University Hospital, Theodor-Stern-Kai 7, 60590 Frankfurt, Germany. arlinghaus@med.uni-frankfurt.de
Franziska T
FT
Arlinghaus
Johannes A
JA
Eble
D020533:Angiogenesis Inhibitors / Q000737:chemistry / Q000378:metabolism; D000818:Animals; D000925:Anticoagulants / Q000737:chemistry / Q000378:metabolism; D000970:Antineoplastic Agents / Q000737:chemistry / Q000378:metabolism; D001777:Blood Coagulation / Q000187:drug effects; D003435:Crotalid Venoms / Q000737:chemistry / Q000378:metabolism* / Q000633:toxicity; D038982:Integrin alpha2beta1 / Q000037:antagonists & inhibitors; D037181:Lectins, C-Type / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D020836:Protein Structure, Quaternary; D030162:Reptilian Proteins / Q000737:chemistry / Q000378:metabolism; D017819:Viperidae / Q000502:physiology
D020533:Angiogenesis Inhibitors; D000925:Anticoagulants; D000970:Antineoplastic Agents; D003435:Crotalid Venoms; D038982:Integrin alpha2beta1; D037181:Lectins, C-Type; D030162:Reptilian Proteins; C402798:flavocetin A; C119730:rhodocetin; C028890:convulxin