AI Article Synopsis
- The interaction between thrombin and platelet glycoprotein Ibalpha (GPIb alpha) is crucial for effective platelet activation.
- The crystal structures show that GPIb alpha binds to thrombin at two specific sites (exosites I and II), but the nature of this interaction varies between different studies.
- The new findings highlight the potential implications for thrombus formation due to the way thrombin interacts with GPIb alpha.
Article Abstract
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.
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| http://dx.doi.org/10.1016/j.molmed.2003.09.009 | DOI Listing |
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