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Thrombin (Factor IIa)

Introduction

spinqualitylabelsall models Thrombin (Factor IIa) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Thrombin is a Trypsin like Serine protease (1). It uses the serine amino acid to specifically cleave fibrinogen into fibrin (3).This forms a blood clot which stops blood from leaking out of the blood circulatory system in case of a rupture. It also catalyzes the activation of factor XIII which stabilizes the fibrin network (3).

Structure

The thrombin molecular structure can be divided into two chains. The first chain (chain A) has 36 residues and is non-essential for proteolytic activities. The second chain (chain B) has a total of 259 amino acid residues and is derived from the carboxyl terminal sequence of prothrombin (2).

Mechanism of action

Applications

References

Source 1: http://www.rcsb.org/pdb/101/motm.do?momID=25

Source 2: http://serpins.med.unc.edu/~fcc/ResearchPicts2006/Thrombin.html

Source 3: Widmaier, Eric P., Hershel Raff, Kevin T. Strang, and Arthur J. Vander. "Cardiovascular Physiology." Vander's Human Physiology: The Mechanisms of Body Function. Boston: McGraw-Hill Higher Education, 2008. 423-27. Print.

Source 4: http://www.sigmaaldrich.com/life-science/metabolomics/enzyme-explorer/analytical-enzymes/fibrinogen-and-fibrin.html

Source 5: http://www.pdb.org/pdb/101/motm_disscussed_entry.do?id=1ppb