Thrombin interaction with platelet membrane glycoprotein Ib alpha.
The interaction of thrombin with platelet glycoprotein Ibalpha (GPIb alpha) is required for optimal platelet activation. The crystal structures of platelet GPIb alpha bound to thrombin reported by Dumas et al. and Celikel et al. both reveal the simultaneous interaction of GPIb alpha with thrombin exosites I and II but differ markedly regarding how the two proteins interact. The possible consequences on thrombus formation of thrombin interacting with GPIb alpha are discussed in light of these new data.
Adam
Frédéric
F
INSERM E348, Faculté de Médecine Xavier Bichat, 16 rue Henri Huchard, 75870 Paris Cedex 18, France.
Bouton
Marie-Christine
MC
Huisse
Marie-Geneviève
MG
Jandrot-Perrus
Martine
M
D000818:Animals; D001777:Blood Coagulation / Q000502:physiology; D001792:Blood Platelets / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism*; D006801:Humans; D010766:Phosphorylation; D019038:Platelet Glycoprotein GPIb-IX Complex / Q000378:metabolism*; D013917:Thrombin / Q000378:metabolism*
D019038:Platelet Glycoprotein GPIb-IX Complex; D013917:Thrombin