1ook
From Proteopedia
(New page: 200px<br /> <applet load="1ook" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ook, resolution 2.30Å" /> '''Crystal Structure o...) |
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| - | [[Image:1ook.gif|left|200px]]<br /> | + | [[Image:1ook.gif|left|200px]]<br /><applet load="1ook" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1ook" size=" | + | |
caption="1ook, resolution 2.30Å" /> | caption="1ook, resolution 2.30Å" /> | ||
'''Crystal Structure of the Complex of Platelet Receptor GPIb-alpha and Human alpha-Thrombin'''<br /> | '''Crystal Structure of the Complex of Platelet Receptor GPIb-alpha and Human alpha-Thrombin'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Thrombin bound to platelets contributes to stop bleeding and, in | + | 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== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1OOK is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with NAG and CL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Thrombin Thrombin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.5 3.4.21.5] Full crystallographic information is available from [http:// | + | 1OOK is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NAG:'>NAG</scene> and <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Thrombin Thrombin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.5 3.4.21.5] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OOK OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Thrombin]] | [[Category: Thrombin]] | ||
[[Category: Celikel, R.]] | [[Category: Celikel, R.]] | ||
| - | [[Category: Ruggeri, Z | + | [[Category: Ruggeri, Z M.]] |
| - | [[Category: Varughese, K | + | [[Category: Varughese, K I.]] |
[[Category: CL]] | [[Category: CL]] | ||
[[Category: NAG]] | [[Category: NAG]] | ||
[[Category: leucine rich repeats]] | [[Category: leucine rich repeats]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:19:58 2008'' |
Revision as of 12:19, 21 February 2008
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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 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 and 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
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