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3osl

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[[Image:3osl.png|left|200px]]
 
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{{STRUCTURE_3osl| PDB=3osl | SCENE= }}
{{STRUCTURE_3osl| PDB=3osl | SCENE= }}
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===Structure of bovine thrombin-activatable fibrinolysis inhibitor in complex with tick carboxypeptidase inhibitor===
===Structure of bovine thrombin-activatable fibrinolysis inhibitor in complex with tick carboxypeptidase inhibitor===
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{{ABSTRACT_PUBMED_20880845}}
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==Function==
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[[http://www.uniprot.org/uniprot/CBPB2_BOVIN CBPB2_BOVIN]] Cleaves C-terminal arginine or lysine residues from biologically active peptides such as kinins or anaphylatoxins in the circulation thereby regulating their activities. Down-regulates fibrinolysis by removing C-terminal lysine residues from fibrin that has already been partially degraded by plasmin.
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{{ABSTRACT_PUBMED_20880845}}
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==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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<ref group="xtra">PMID:20880845</ref><ref group="xtra">PMID:20088943</ref><ref group="xtra">PMID:18722183</ref><references group="xtra"/>
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<ref group="xtra">PMID:020880845</ref><ref group="xtra">PMID:020088943</ref><ref group="xtra">PMID:018722183</ref><references group="xtra"/><references/>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Carboxypeptidase U]]
[[Category: Carboxypeptidase U]]

Revision as of 08:37, 2 May 2013

Template:STRUCTURE 3osl

Contents

Structure of bovine thrombin-activatable fibrinolysis inhibitor in complex with tick carboxypeptidase inhibitor

Template:ABSTRACT PUBMED 20880845

Function

[CBPB2_BOVIN] Cleaves C-terminal arginine or lysine residues from biologically active peptides such as kinins or anaphylatoxins in the circulation thereby regulating their activities. Down-regulates fibrinolysis by removing C-terminal lysine residues from fibrin that has already been partially degraded by plasmin.

About this Structure

3osl is a 4 chain structure with sequence from Bos taurus and Rhipicephalus bursa. Full crystallographic information is available from OCA.

Reference

  • Valnickova Z, Sanglas L, Arolas JL, Petersen SV, Schar C, Otzen D, Aviles FX, Gomis-Ruth FX, Enghild JJ. Flexibility of the thrombin-activatable fibrinolysis inhibitor pro-domain enables productive binding of protein substrates. J Biol Chem. 2010 Dec 3;285(49):38243-50. Epub 2010 Sep 29. PMID:20880845 doi:10.1074/jbc.M110.150342
  • Sanglas L, Arolas JL, Valnickova Z, Aviles FX, Enghild JJ, Gomis-Ruth FX. Insights into the molecular inactivation mechanism of human activated thrombin-activatable fibrinolysis inhibitor. J Thromb Haemost. 2010 May;8(5):1056-65. Epub 2010 Jan 17. PMID:20088943 doi:10.1111/j.1538-7836.2010.03740.x
  • Sanglas L, Valnickova Z, Arolas JL, Pallares I, Guevara T, Sola M, Kristensen T, Enghild JJ, Aviles FX, Gomis-Ruth FX. Structure of activated thrombin-activatable fibrinolysis inhibitor, a molecular link between coagulation and fibrinolysis. Mol Cell. 2008 Aug 22;31(4):598-606. PMID:18722183 doi:10.1016/j.molcel.2008.05.031

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