1oc0

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(New page: 200px<br /> <applet load="1oc0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1oc0, resolution 2.28&Aring;" /> '''PLASMINOGEN ACTIVAT...)
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'''PLASMINOGEN ACTIVATOR INHIBITOR-1 COMPLEX WITH SOMATOMEDIN B DOMAIN OF VITRONECTIN'''<br />
'''PLASMINOGEN ACTIVATOR INHIBITOR-1 COMPLEX WITH SOMATOMEDIN B DOMAIN OF VITRONECTIN'''<br />
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==About this Structure==
==About this Structure==
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1OC0 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OC0 OCA].
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1OC0 is a [http://en.wikipedia.org/wiki/Protein_complex 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=1OC0 OCA].
==Reference==
==Reference==
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[[Category: serpin]]
[[Category: serpin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:31:23 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:33:45 2008''

Revision as of 14:33, 15 February 2008


1oc0, resolution 2.28Å

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

Contents

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.

Disease

Known diseases associated with this structure: Hemorrhagic diathesis due to PAI1 deficiency OMIM:[173360], Thrombophilia due to excessive plasminogen activator inhibitor OMIM:[173360]

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

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