Thrombin allostery

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

doi:10.1039/b616819a

Thrombin allostery

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

Biochemistry & Molecular Biology

Upstate Medical University

Washington University St. Louis

Research output: Contribution to journal › Review article › peer-review

46 Scopus citations

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. This journal is

Original language	English
Pages (from-to)	1292-1306
Number of pages	15
Journal	Physical Chemistry Chemical Physics
Volume	9
Issue number	11
DOIs	https://doi.org/10.1039/b616819a
State	Published - 2007

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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. This journal is",

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AU - Di Cera, Enrico

AU - Page, Michael J.

AU - Bah, Alaji

AU - Bush-Pelc, Leslie A.

AU - Garvey, Laura C.

PY - 2007

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AB - 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. This journal is

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JO - Physical Chemistry Chemical Physics

JF - Physical Chemistry Chemical Physics

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Thrombin allostery

Abstract

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