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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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| Опубликовано в: : | J Biol Chem |
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| Главные авторы: | , , , , , , , |
| Формат: | Artigo |
| Язык: | Inglês |
| Опубликовано: |
American Society for Biochemistry and Molecular Biology
2014
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| Предметы: | |
| 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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