1jou

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spinqualitylabelsall models PDB ID 1jou Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
, resolution 1.80Å
Ligands:	, , and
Coordinates:	save as pdb, mmCIF, xml

Crystal Structure of Native S195A Thrombin with an Unoccupied Active Site

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

Thrombin participates in its own positive and negative feedback loops, and its allosteric state helps determine the hemostatic balance. Here we present the 1.8 A crystallographic structure of S195A thrombin in two conformational states: active site occupied and active site free. The active site-occupied form shows how thrombin can accommodate substrates, such as protein C. The active site-free form is in a previously unobserved closed conformation of thrombin, which satisfies all the conditions of the so-called "slow" form. A mechanism of allostery is revealed, which relies on the concerted movement of the disulphide bond between Cys168 and 182 and aromatic residues Phe227, Trp215, and Trp60d. These residues constitute an allosteric switch, which is flipped directly through sodium binding, resulting in the fast form with an open active site.

Disease

Known diseases associated with this structure: Dysprothrombinemia OMIM:[176930], Hyperprothrombinemia OMIM:[176930], Hypoprothrombinemia OMIM:[176930]

About this Structure

1JOU is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

The molecular basis of thrombin allostery revealed by a 1.8 A structure of the "slow" form., Huntington JA, Esmon CT, Structure. 2003 Apr;11(4):469-79. PMID:12679024

Page seeded by OCA on Thu Mar 20 12:06:20 2008