Crystal Structure of the GpIbα-Thrombin Complex Essential for Platelet Aggregation
In: Science, Jg. 301 (2003-07-11), S. 222-226
Online
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Zugriff:
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.
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Crystal Structure of the GpIbα-Thrombin Complex Essential for Platelet Aggregation
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Autor/in / Beteiligte Person: | Seehra, Jasbir ; Dumas, John J. ; Somers, William S. ; Kumar, Ravindra ; Mosyak, Lidia |
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Zeitschrift: | Science, Jg. 301 (2003-07-11), S. 222-226 |
Veröffentlichung: | American Association for the Advancement of Science (AAAS), 2003 |
Medientyp: | unknown |
ISSN: | 1095-9203 (print) ; 0036-8075 (print) |
DOI: | 10.1126/science.1083917 |
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