1p9a
From Proteopedia
(New page: 200px<br /> <applet load="1p9a" size="450" color="white" frame="true" align="right" spinBox="true" caption="1p9a, resolution 1.7Å" /> '''Crystal Structure of...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1p9a. | + | [[Image:1p9a.jpg|left|200px]]<br /><applet load="1p9a" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1p9a" size=" | + | |
caption="1p9a, resolution 1.7Å" /> | caption="1p9a, resolution 1.7Å" /> | ||
'''Crystal Structure of N-Terminal Domain of Human Platelet Receptor Glycoprotein Ib-alpha at 1.7 Angstrom Resolution'''<br /> | '''Crystal Structure of N-Terminal Domain of Human Platelet Receptor Glycoprotein Ib-alpha at 1.7 Angstrom Resolution'''<br /> | ||
| Line 11: | Line 10: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1P9A is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1P9A is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P9A OCA]. |
==Reference== | ==Reference== | ||
| Line 24: | Line 23: | ||
[[Category: platelet receptors]] | [[Category: platelet receptors]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:39:23 2008'' |
Revision as of 14:39, 15 February 2008
|
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 Fri Feb 15 16:39:23 2008
