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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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Библиографические подробности
Опубликовано в: :J Biol Chem
Главные авторы: Izaguirre, Gonzalo, Aguila, Sonia, Qi, Lixin, Swanson, Richard, Roth, Ryan, Rezaie, Alireza R., Gettins, Peter G. W., Olson, Steven T.
Формат: Artigo
Язык:Inglês
Опубликовано: American Society for Biochemistry and Molecular Biology 2014
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Online-ссылка: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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