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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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| Vydáno v: | J Biol Chem |
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| Hlavní autoři: | , , , , , , , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
American Society for Biochemistry and Molecular Biology
2014
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| Témata: | |
| On-line přístup: | 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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