1ook
From Proteopedia
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'''Crystal Structure of the Complex of Platelet Receptor GPIb-alpha and Human alpha-Thrombin''' | '''Crystal Structure of the Complex of Platelet Receptor GPIb-alpha and Human alpha-Thrombin''' | ||
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[[Category: Ruggeri, Z M.]] | [[Category: Ruggeri, Z M.]] | ||
[[Category: Varughese, K I.]] | [[Category: Varughese, K I.]] | ||
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Revision as of 01:06, 3 May 2008
Crystal Structure of the Complex of Platelet Receptor GPIb-alpha and Human alpha-Thrombin
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 disease associated with this structure: Bernard-Soulier syndrome, type A OMIM:[606672], von Willebrand disease, platelet-type OMIM:[606672], Nonarteritic anterior ischemic optic neuropathy, susceptibility to OMIM:[606672]
About this Structure
1OOK is a Protein complex structure of sequences 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 Sat May 3 04:06:17 2008