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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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| Publicado no: | J Biol Chem |
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| Main Authors: | , , , , , , , |
| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
American Society for Biochemistry and Molecular Biology
2014
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| Assuntos: | |
| Acesso em linha: | 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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