Conformational Activation of Antithrombin by Heparin Involves an Altered Exosite Interaction with Protease

Heparin allosterically activates antithrombin as an inhibitor of factors Xa and IXa by enhancing the initial Michaelis complex interaction of inhibitor with protease through exosites. Here, we investigate the mechanism of this enhancement by analyzing the effects of alanine mutations of six putative...

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Détails bibliographiques
Publié dans:J Biol Chem
Auteurs principaux: Izaguirre, Gonzalo, Aguila, Sonia, Qi, Lixin, Swanson, Richard, Roth, Ryan, Rezaie, Alireza R., Gettins, Peter G. W., Olson, Steven T.
Format: Artigo
Langue:Inglês
Publié: American Society for Biochemistry and Molecular Biology 2014
Sujets:
Enzymology
Accès en ligne:https://ncbi.nlm.nih.gov/pmc/articles/PMC4256340/
https://ncbi.nlm.nih.gov/pubmed/25331949
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M114.611707
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