1p9a
From Proteopedia
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Crystal Structure of N-Terminal Domain of Human Platelet Receptor Glycoprotein Ib-alpha at 1.7 Angstrom Resolution
Contents |
Overview
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.
Disease
Known diseases associated with this structure: Bernard-Soulier syndrome, type A OMIM:[606672], Nonarteritic anterior ischemic optic neuropathy, susceptibility to OMIM:[606672], von Willebrand disease, platelet-type OMIM:[606672]
About this Structure
1P9A is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Modulation of alpha-thrombin function by distinct interactions with platelet glycoprotein Ibalpha., Celikel R, McClintock RA, Roberts JR, Mendolicchio GL, Ware J, Varughese KI, Ruggeri ZM, Science. 2003 Jul 11;301(5630):218-21. PMID:12855810
Page seeded by OCA on Mon Nov 12 18:41:16 2007
