Article
Modulation of alpha-thrombin function by distinct interactions with platelet glycoprotein Ibalpha.
Science (New York, N.Y.) - 11 Jul 2003
Celikel Reha, McClintock Richard A, Roberts James R, Mendolicchio G Loredana, Ware Jerry, Varughese Kottayil I, Ruggeri Zaverio M
Abstract excerpt
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...
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