Crystal structure of the GpIbalpha-thrombin complex essential for platelet aggregation
- PMID: 12855811
- DOI: 10.1126/science.1083917
Crystal structure of the GpIbalpha-thrombin complex essential for platelet aggregation
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.
Comment in
-
Structural biology. A ménage à trois in two configurations.Science. 2003 Jul 11;301(5630):177-9. doi: 10.1126/science.1087734. Science. 2003. PMID: 12855796 No abstract available.
MeSH terms
Substances
Associated data
- Actions
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases