Jump to main content
Jump to site search

Issue 11, 2007
Previous Article Next Article

Thrombin allostery

Author affiliations

Abstract

Thrombin is a Na+-activated, allosteric serine protease that plays multiple functional roles in blood pathophysiology. Binding of Na+ is the major driving force behind the procoagulant, prothrombotic and signaling functions of the enzyme. This review summarizes our current understanding of the molecular basis of thrombin allostery with special emphasis on the kinetic aspects of Na+ activation. The molecular mechanism of thrombin allostery is a remarkable example of long-range communication that offers a paradigm for many other biological systems.

Graphical abstract: Thrombin allostery

Back to tab navigation

Article information


Submitted
17 Nov 2006
Accepted
11 Dec 2006
First published
12 Jan 2007

Phys. Chem. Chem. Phys., 2007,9, 1291-1306
Article type
Invited Article

Thrombin allostery

E. Di Cera, M. J. Page, A. Bah, L. A. Bush-Pelc and L. C. Garvey, Phys. Chem. Chem. Phys., 2007, 9, 1291
DOI: 10.1039/B616819A

Social activity

Search articles by author

Spotlight

Advertisements