1dvn

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[[Image:1dvn.png|left|200px]]
 
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{{STRUCTURE_1dvn| PDB=1dvn | SCENE= }}
{{STRUCTURE_1dvn| PDB=1dvn | SCENE= }}
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===LATENT FORM OF PLASMINOGEN ACTIVATOR INHIBITOR-1 (PAI-1)===
===LATENT FORM OF PLASMINOGEN ACTIVATOR INHIBITOR-1 (PAI-1)===
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{{ABSTRACT_PUBMED_10913251}}
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{{ABSTRACT_PUBMED_10913251}}
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==Disease==
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[[http://www.uniprot.org/uniprot/PAI1_HUMAN PAI1_HUMAN]] Defects in SERPINE1 are the cause of plasminogen activator inhibitor-1 deficiency (PAI-1D) [MIM:[http://omim.org/entry/613329 613329]]. It is a hematologic disorder characterized by increased bleeding after trauma, injury, or surgery. Affected females have menorrhagia. The bleeding defect is due to increased fibrinolysis of fibrin blood clots due to deficiency of plasminogen activator inhibitor-1, which inhibits tissue and urinary activators of plasminogen.<ref>PMID:9207454</ref> Note=High concentrations of SERPINE1 seem to contribute to the development of venous but not arterial occlusions.
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==Function==
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[[http://www.uniprot.org/uniprot/PAI1_HUMAN PAI1_HUMAN]] Serine protease inhibitor. This inhibitor acts as 'bait' for tissue plasminogen activator, urokinase, protein C and matriptase-3/TMPRSS7. Its rapid interaction with PLAT may function as a major control point in the regulation of fibrinolysis.<ref>PMID:15853774</ref>
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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<ref group="xtra">PMID:010913251</ref><ref group="xtra">PMID:014695246</ref><references group="xtra"/>
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<ref group="xtra">PMID:010913251</ref><ref group="xtra">PMID:014695246</ref><references group="xtra"/><references/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Buckley, D I.]]
[[Category: Buckley, D I.]]

Revision as of 20:05, 24 March 2013

Template:STRUCTURE 1dvn

Contents

LATENT FORM OF PLASMINOGEN ACTIVATOR INHIBITOR-1 (PAI-1)

Template:ABSTRACT PUBMED 10913251

Disease

[PAI1_HUMAN] Defects in SERPINE1 are the cause of plasminogen activator inhibitor-1 deficiency (PAI-1D) [MIM:613329]. It is a hematologic disorder characterized by increased bleeding after trauma, injury, or surgery. Affected females have menorrhagia. The bleeding defect is due to increased fibrinolysis of fibrin blood clots due to deficiency of plasminogen activator inhibitor-1, which inhibits tissue and urinary activators of plasminogen.[1] Note=High concentrations of SERPINE1 seem to contribute to the development of venous but not arterial occlusions.

Function

[PAI1_HUMAN] Serine protease inhibitor. This inhibitor acts as 'bait' for tissue plasminogen activator, urokinase, protein C and matriptase-3/TMPRSS7. Its rapid interaction with PLAT may function as a major control point in the regulation of fibrinolysis.[2]

About this Structure

1dvn is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

See Also

Reference

  • Stout TJ, Graham H, Buckley DI, Matthews DJ. Structures of active and latent PAI-1: a possible stabilizing role for chloride ions. Biochemistry. 2000 Jul 25;39(29):8460-9. PMID:10913251
  • Sandelin E. On hydrophobicity and conformational specificity in proteins. Biophys J. 2004 Jan;86(1 Pt 1):23-30. PMID:14695246 doi:10.1016/S0006-3495(04)74080-1
  1. ↑ Fay WP, Parker AC, Condrey LR, Shapiro AD. Human plasminogen activator inhibitor-1 (PAI-1) deficiency: characterization of a large kindred with a null mutation in the PAI-1 gene. Blood. 1997 Jul 1;90(1):204-8. PMID:9207454
  2. ↑ Szabo R, Netzel-Arnett S, Hobson JP, Antalis TM, Bugge TH. Matriptase-3 is a novel phylogenetically preserved membrane-anchored serine protease with broad serpin reactivity. Biochem J. 2005 Aug 15;390(Pt 1):231-42. PMID:15853774 doi:BJ20050299

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