Thrombin allostery

Enrico Di Cera; Michael J. Page; Alaji Bah; Leslie A. Bush-Pelc; Laura C. Garvey

doi:10.1039/B616819A

skip RSC | ChemSpider | Feedback

Home > Journals > Physical Chemistry Chem... > Thrombin allostery

Authors & Referees | Librarians

You do not have JavaScript enabled. Please enable JavaScript to access the full features of the site or access our non-JavaScript page.

Physical Chemistry Chemical Physics

Issue 11, 2007

Partner Societies
More about this Journal
Editorial Board
Submit an Article

Follow Journal | |

Journal Home | RSC Journals

Invited Article

Previous Article | Next Article

Thrombin allostery

Enrico Di Cera , Michael J. Page , Alaji Bah , Leslie A. Bush-Pelc and Laura C. Garvey

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

DOI: 10.1039/B616819A
Received 17 Nov 2006, Accepted 11 Dec 2006
First published on the web 12 Jan 2007

Please wait while Download options loads

Request Permissions

Abstract
Cited by
Related Content

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.

Articles By

Enrico Di Cera
Michael J. Page
Alaji Bah
Leslie A. Bush-Pelc
Laura C. Garvey

Terms & Conditions|Privacy |Accessibility|ACAP Enabled

Physical Chemistry Chemical Physics

Thrombin allostery

Log in (Free Access)

Log in (Subscriber Access)

Articles By