1ook
From Proteopedia
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Crystal Structure of the Complex of Platelet Receptor GPIb-alpha and Human alpha-Thrombin
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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], Dysprothrombinemia OMIM:[176930], Hyperprothrombinemia OMIM:[176930], Hypoprothrombinemia OMIM:[176930], Nonarteritic anterior ischemic optic neuropathy, susceptibility to OMIM:[606672], von Willebrand disease, platelet-type OMIM:[606672]
About this Structure
1OOK is a Protein complex structure of sequences from Homo sapiens with NAG and CL as ligands. Active as Thrombin, with EC number 3.4.21.5 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 18:34:57 2007
