1P8V
CRYSTAL STRUCTURE OF THE COMPLEX OF PLATELET RECEPTOR GPIB-ALPHA AND ALPHA-THROMBIN AT 2.6A
1P8V の概要
| エントリーDOI | 10.2210/pdb1p8v/pdb |
| 分子名称 | Platelet glycoprotein Ib alpha chain, Prothrombin, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, ... (7 entities in total) |
| 機能のキーワード | platelet glycoprotein receptor, leucine rich repeat domain, membrane protein-hydrolase complex, membrane protein/hydrolase |
| 由来する生物種 | Homo sapiens (human) 詳細 |
| タンパク質・核酸の鎖数 | 3 |
| 化学式量合計 | 65037.33 |
| 構造登録者 | Dumas, J.J.,Kumar, R.,Seehra, J.,Somers, W.S.,Mosyak, L. (登録日: 2003-05-07, 公開日: 2003-07-22, 最終更新日: 2024-12-25) |
| 主引用文献 | 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 Cited by 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: 12855811DOI: 10.1126/science.1083917 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.6 Å) |
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