Issue 11, 2007
From the journal:

Physical Chemistry Chemical Physics

Thrombin allostery†‡

Enrico Di Cera,*a   Michael J. Page,a   Alaji Bah,a   Leslie A. Bush-Pelca  and  Laura C. Garveya  

* Corresponding authors

a Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, Box 8231, St. Louis
E-mail: enrico@wustl.edu
Fax: +1 (314) 362-4311
Tel: +1 (314) 362-4185

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

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Article information

DOI
https://doi.org/10.1039/B616819A
Article type
Invited Article
Submitted
17 Nov 2006
Accepted
11 Dec 2006
First published
12 Jan 2007

Phys. Chem. Chem. Phys., 2007,9, 1291-1306

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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

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