1ook

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1ook.gif|left|200px]]<br /><applet load="1ook" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1ook.gif|left|200px]]
-
caption="1ook, resolution 2.30&Aring;" />
+
 
-
'''Crystal Structure of the Complex of Platelet Receptor GPIb-alpha and Human alpha-Thrombin'''<br />
+
{{Structure
 +
|PDB= 1ook |SIZE=350|CAPTION= <scene name='initialview01'>1ook</scene>, resolution 2.30&Aring;
 +
|SITE=
 +
|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> and <scene name='pdbligand=CL:CHLORIDE ION'>CL</scene>
 +
|ACTIVITY= [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]
 +
|GENE= GP1BA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
 +
}}
 +
 
 +
'''Crystal Structure of the Complex of Platelet Receptor GPIb-alpha and Human alpha-Thrombin'''
 +
 
==Overview==
==Overview==
Line 10: Line 19:
==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 <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].
+
1OOK is a [[Protein complex]] structure of sequences 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=1OOK OCA].
==Reference==
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12855810 12855810]
+
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:[http://www.ncbi.nlm.nih.gov/pubmed/12855810 12855810]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
Line 22: Line 31:
[[Category: CL]]
[[Category: CL]]
[[Category: NAG]]
[[Category: NAG]]
-
[[Category: leucine rich repeats]]
+
[[Category: leucine rich repeat]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:19:58 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:13:37 2008''

Revision as of 11:13, 20 March 2008


PDB ID 1ook

Drag the structure with the mouse to rotate
, resolution 2.30Å
Ligands: and
Gene: GP1BA (Homo sapiens)
Activity: Thrombin, with EC number 3.4.21.5
Coordinates: save as pdb, mmCIF, xml



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. 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 Thu Mar 20 13:13:37 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools