The Allosteric Mechanism of Activation of Antithrombin as an Inhibitor of Factor IXa and Factor Xa: HEPARIN-INDEPENDENT FULL ACTIVATION THROUGH MUTATIONS ADJACENT TO HELIX D

Allosteric conformational changes in antithrombin induced by binding a specific heparin pentasaccharide result in very large increases in the rates of inhibition of factors IXa and Xa but not of thrombin. These are accompanied by CD, fluorescence, and NMR spectroscopic changes. X-ray structures show...

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Detalhes bibliográficos
Main Authors: Dementiev, Alexey, Swanson, Richard, Roth, Ryan, Isetti, Giulia, Izaguirre, Gonzalo, Olson, Steven T., Gettins, Peter G. W.
Formato: Artigo
Idioma:Inglês
Publicado em: American Society for Biochemistry and Molecular Biology 2013
Assuntos:
Enzymology
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC3837108/
https://ncbi.nlm.nih.gov/pubmed/24068708
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M113.510727
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