1oc0: Difference between revisions
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{{STRUCTURE_1oc0| PDB=1oc0 | SCENE= }} | |||
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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.]] | ||
[[Category: | [[Category: Cell migration]] | ||
[[Category: | [[Category: Fibrinolysis]] | ||
[[Category: | [[Category: Plasminogen activation,heparin-binding,cell adhesion]] | ||
[[Category: | [[Category: Proteinase inhibitor]] | ||
[[Category: | [[Category: Serpin]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:38:58 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 03:39, 3 May 2008
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| 1oc0, resolution 2.28Å () | |||||||||
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| Related: | 1a7c, 1b3k, 1c5g, 1db2, 1dvm, 1dvn, 1lj5, 9pai | ||||||||
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| Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
PLASMINOGEN ACTIVATOR INHIBITOR-1 COMPLEX WITH SOMATOMEDIN B DOMAIN OF VITRONECTIN
OverviewOverview
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 StructureAbout this Structure
1OC0 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
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