1P8V

CRYSTAL STRUCTURE OF THE COMPLEX OF PLATELET RECEPTOR GPIB-ALPHA AND ALPHA-THROMBIN AT 2.6A

Summary for 1P8V

• Entry DOI: 10.2210/pdb1p8v/pdb
• Descriptor: Platelet glycoprotein Ib alpha chain, Prothrombin, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, ... (7 entities in total)
• Functional Keywords: platelet glycoprotein receptor, leucine rich repeat domain, membrane protein-hydrolase complex, membrane protein/hydrolase
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 3
• Total formula weight: 65037.33

Authors

Dumas, J.J.,Kumar, R.,Seehra, J.,Somers, W.S.,Mosyak, L. (deposition date: 2003-05-07, release date: 2003-07-22, Last modification date: 2021-10-27)

Primary citation

Dumas, J.J.,Kumar, R.,Seehra, J.,Somers, W.S.,Mosyak, L.
Crystal Structure of the GpIbalpha-Thrombin Complex Essential for Platelet Aggregation
Science, 301:222-226, 2003

PubMed 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.

PubMed: 12855811
DOI: 10.1126/science.1083917

Experimental method

X-RAY DIFFRACTION (2.6 Å)