1oc0: Difference between revisions
New page: left|200px<br /> <applet load="1oc0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1oc0, resolution 2.28Å" /> '''PLASMINOGEN ACTIVAT... |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1oc0. | [[Image:1oc0.jpg|left|200px]]<br /><applet load="1oc0" size="350" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="1oc0" size=" | |||
caption="1oc0, resolution 2.28Å" /> | caption="1oc0, resolution 2.28Å" /> | ||
'''PLASMINOGEN ACTIVATOR INHIBITOR-1 COMPLEX WITH SOMATOMEDIN B DOMAIN OF VITRONECTIN'''<br /> | '''PLASMINOGEN ACTIVATOR INHIBITOR-1 COMPLEX WITH SOMATOMEDIN B DOMAIN OF VITRONECTIN'''<br /> | ||
| Line 11: | Line 10: | ||
==About this Structure== | ==About this Structure== | ||
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:// | 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== | ||
| Line 30: | Line 29: | ||
[[Category: serpin]] | [[Category: serpin]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:33:45 2008'' | ||
Revision as of 17:33, 15 February 2008
|
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.
DiseaseDisease
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 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 Fri Feb 15 16:33:45 2008