期刊
SCIENCE
卷 301, 期 5630, 页码 218-221出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1084183
关键词
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资金
- NCRR NIH HHS [RR0833] Funding Source: Medline
- NHLBI NIH HHS [HL-31950, R01 HL042846, HL-42846, HL-55375, HL-48728] Funding Source: Medline
Thrombin bound to platelets contributes to stop bleeding and, in pathological conditions, may cause vascular thrombosis. We have determined the structure of platelet glycoprotein Ibalpha (GpIbalpha) bound to thrombin at 2.3 angstrom resolution and defined two sites in GpIbalpha that bind to exosite II and exosite I of two distinct alpha-thrombin molecules, respectively. GpIbalpha occupancy may be sequential, as the site binding to alpha-thrombin exosite I appears to be cryptic in the unoccupied receptor but exposed when a first thrombin molecule is bound through exosite II. These interactions may modulate alpha-thrombin function by mediating GpIbalpha clustering and cleavage of protease-activated receptors, which promote platelet activation, while limiting fibrinogen clotting through blockade of exosite I.
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