Publication:
Conformational activation of antithrombin by heparin involves an altered exosite interaction with protease

Thumbnail Image
Files
PIIS0021925820473569.pdf(3.49 MB)
Date
2014-12-05
relationships.isAuthorOfPublication
Profile Picture
Person
relationships.isSecondaryAuthorOf
relationships.isDirectorOf
Authors
Águila Martínez, Sonia ; Izaguirre, Gonzalo ; Qi, Lixin ; Swanson, Richard ; Roth, Ryan ; Rezaie, Alireza R. ; Gettins, Peter G. W. ; Olson, Steven T.
item.page.secondaryauthor
item.page.director
Publisher
Elsevier; American Society for Biochemistry and Molecular Biology
publication.page.editor
publication.page.department
Medicina Interna
DOI
https://doi.org/10.1074/jbc.M114.611707
item.page.type
info:eu-repo/semantics/article
Description
Abstract
Background: Exosites are known to mediate heparin allosteric activation of antithrombin. Results: Mutagenesis revealed that an exosite differentially contributes to antithrombin reactivity with factors Xa/IXa in unactivated and heparin-activated states. Conclusion: Heparin allosteric activation of antithrombin results from alterations in an exosite interaction with protease induced by core conformational changes. Significance: The findings support our recently proposed model of antithrombin allosteric activation.
publication.page.subject
Allosteric Regulation , Antithrombin (AT) , Heparin , Protease , Serpin , Anticoagulant , Blood Coagulation , Exosite
Citation
The Journal of Biological Chemistry VOL. 289, NO. 49, pp. 34049–34064
URI
http://hdl.handle.net/10201/205341
item.page.embargo
Collections
Artículos
Ir a Estadísticas