9qrv
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Crystal Structure of an anti-VWF CK Domain Fab in Complex with the C-Terminal CK Domain of Cynomolgus Monkey von Willebrand Factor.
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Structural highlights
FunctionA0A2K5X4G5_MACFA Important in the maintenance of hemostasis, it promotes adhesion of platelets to the sites of vascular injury by forming a molecular bridge between sub-endothelial collagen matrix and platelet-surface receptor complex GPIb-IX-V. Also acts as a chaperone for coagulation factor VIII, delivering it to the site of injury, stabilizing its heterodimeric structure and protecting it from premature clearance from plasma.[ARBA:ARBA00055715][PIRNR:PIRNR002495] Important in the maintenance of hemostasis, it promotes adhesion of platelets to the sites of vascular injury by forming a molecular bridge between sub-endothelial collagen matrix and platelet-surface receptor complex, glycoprotein Ibalpha/IX/V. Also acts as a chaperone for coagulation factor VIII, delivering it to the site of injury, stabilizing its heterodimeric structure and protecting it from premature clearance from plasma.[ARBA:ARBA00059961] Contents | ||||||||||||||||||||
This page was last modified 07:24, 11 February 2026.