1oc0

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{{Structure
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|PDB= 1oc0 |SIZE=350|CAPTION= <scene name='initialview01'>1oc0</scene>, resolution 2.28&Aring;
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{{STRUCTURE_1oc0| PDB=1oc0 | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1oc0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oc0 OCA], [http://www.ebi.ac.uk/pdbsum/1oc0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1oc0 RCSB]</span>
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'''PLASMINOGEN ACTIVATOR INHIBITOR-1 COMPLEX WITH SOMATOMEDIN B DOMAIN OF VITRONECTIN'''
'''PLASMINOGEN ACTIVATOR INHIBITOR-1 COMPLEX WITH SOMATOMEDIN B DOMAIN OF VITRONECTIN'''
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[[Category: Read, R J.]]
[[Category: Read, R J.]]
[[Category: Zhou, A.]]
[[Category: Zhou, A.]]
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[[Category: cell migration]]
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[[Category: Cell migration]]
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[[Category: fibrinolysis]]
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[[Category: Fibrinolysis]]
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[[Category: plasminogen activation,heparin-binding,cell adhesion]]
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[[Category: Plasminogen activation,heparin-binding,cell adhesion]]
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[[Category: proteinase inhibitor]]
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[[Category: Proteinase inhibitor]]
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[[Category: serpin]]
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[[Category: Serpin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:38:58 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:42:59 2008''
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Revision as of 00:39, 3 May 2008


PDB ID 1oc0

Drag the structure with the mouse to rotate
1oc0, resolution 2.28Å ()
Related: 1a7c, 1b3k, 1c5g, 1db2, 1dvm, 1dvn, 1lj5, 9pai
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml



PLASMINOGEN ACTIVATOR INHIBITOR-1 COMPLEX WITH SOMATOMEDIN B DOMAIN OF VITRONECTIN


Overview

The interaction of the plasma protein vitronectin with plasminogen activator inhibitor-1 (PAI-1) is central to human health. Vitronectin binding extends the lifetime of active PAI-1, which controls hemostasis by inhibiting fibrinolysis and has also been implicated in angiogenesis. The PAI-1-vitronectin binding interaction also affects cell adhesion and motility. For these reasons, elevated PAI-1 activities are associated both with coronary thrombosis and with a poor prognosis in many cancers. Here we show the crystal structure at a resolution of 2.3 A of the complex of the somatomedin B domain of vitronectin with PAI-1. The structure of the complex explains how vitronectin binds to and stabilizes the active conformation of PAI-1. It also explains the tissue effects of PAI-1, as PAI-1 competes for and sterically blocks the interaction of vitronectin with cell surface receptors and integrins. Structural understanding of the essential biological roles of the interaction between PAI-1 and vitronectin opens the prospect of specifically designed blocking agents for the prevention of thrombosis and treatment of cancer.

About this Structure

1OC0 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

How vitronectin binds PAI-1 to modulate fibrinolysis and cell migration., Zhou A, Huntington JA, Pannu NS, Carrell RW, Read RJ, Nat Struct Biol. 2003 Jul;10(7):541-4. PMID:12808446 Page seeded by OCA on Sat May 3 03:38:58 2008

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