3lms

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Revision as of 23:21, 10 April 2013

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Template:STRUCTURE 3lms

Contents 1 Structure of human activated thrombin-activatable fibrinolysis inhibitor, TAFIa, in complex with tick-derived funnelin inhibitor, TCI. 2 Function 3 About this Structure 4 Reference

Structure of human activated thrombin-activatable fibrinolysis inhibitor, TAFIa, in complex with tick-derived funnelin inhibitor, TCI.

Template:ABSTRACT PUBMED 20088943

Function

[CBPB2_HUMAN] 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.^[1]

About this Structure

3lms is a 2 chain structure with sequence from Homo sapiens and Rhipicephalus bursa. Full crystallographic information is available from OCA.

Reference

• 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

1. ↑ Mao SS, Cooper CM, Wood T, Shafer JA, Gardell SJ. Characterization of plasmin-mediated activation of plasma procarboxypeptidase B. Modulation by glycosaminoglycans. J Biol Chem. 1999 Dec 3;274(49):35046-52. PMID:10574983