3osl
From Proteopedia
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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=== | ||
+ | {{ABSTRACT_PUBMED_20880845}} | ||
- | + | ==Function== | |
- | + | [[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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==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
- | <ref group="xtra">PMID: | + | <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
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
Categories: Bos taurus | Carboxypeptidase U | Rhipicephalus bursa | Arolas, J L. | Aviles, F X. | Enghild, J J. | Gomis-Ruth, F X. | Otzen, D. | Petersen, S V. | Sanglas, L. | Schar, C. | Valnickova, Z. | Alpha/beta-hydrolase-related fold | Blood | Coagulation | Fibrinolysis | Hydrolase-hydrolase inhibitor complex