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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 ex...

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Published in:Trends in molecular medicine 2003-11, Vol.9 (11), p.461-464
Main Authors: Adam, Frédéric, Bouton, Marie-Christine, Huisse, Marie-Geneviève, Jandrot-Perrus, Martine
Format: Article
Language:English
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Summary: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.
ISSN:1471-4914
DOI:10.1016/j.molmed.2003.09.009