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- W2003648675 abstract "Direct interaction between platelet receptor glycoprotein Ibalpha (GpIbalpha) and thrombin is required for platelet aggregation and activation at sites of vascular injury. Abnormal GpIbalpha-thrombin binding is associated with many pathological conditions,including occlusive arterial thrombosis and bleeding disorders. The crystal structure of the GpIbalpha-thrombin complex at 2.6 angstrom resolution reveals simultaneous interactions of GpIbalpha with exosite I of one thrombin molecule,and with exosite II of a second thrombin molecule. In the crystal lattice,the periodic arrangement of GpIbalpha-thrombin complexes mirrors a scaffold that could serve as a driving force for tight platelet adhesion. The details of these interactions reconcile GpIbalpha-thrombin binding modes that are presently controversial,highlighting two distinct interfaces that are potential targets for development of novel antithrombotic drugs." @default.
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- W2003648675 date "2003-07-11" @default.
- W2003648675 modified "2023-10-06" @default.
- W2003648675 title "Crystal Structure of the GpIbα-Thrombin Complex Essential for Platelet Aggregation" @default.
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- W2003648675 doi "https://doi.org/10.1126/science.1083917" @default.
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