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2pw8

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(New page: 200px<br /> <applet load="2pw8" size="450" color="white" frame="true" align="right" spinBox="true" caption="2pw8, resolution 1.840&Aring;" /> '''Crystal structure ...)
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Revision as of 21:21, 12 November 2007

Image:2pw8.gif

2pw8, resolution 1.840Å

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Crystal structure of sulfo-hirudin complexed to thrombin

Contents

Overview

The leech-derived anticoagulant hirudin is post-translationally sulfated, on tyrosine 63, resulting in a >10-fold increase in its affinity for, thrombin. We report the structure of a biosynthetic sulfo-hirudin, complexed to thrombin solved to 1.84 A resolution and show that sulfation, is responsible for a salt bridge and an extended hydrogen-bond network, that taken together account for the increased affinity of sulfo-hirudin, for thrombin. We also identify a divalent cation binding site at the, interface between the two subunits of alpha-thrombin that may modulate the, physiological activity of thrombin.

Disease

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

About this Structure

2PW8 is a Protein complex structure of sequences from Hirudo medicinalis and Homo sapiens with NI and NA as ligands. Full crystallographic information is available from OCA.

Reference

Crystal Structure of a Biosynthetic Sulfo-hirudin Complexed to Thrombin., Liu CC, Brustad E, Liu W, Schultz PG, J Am Chem Soc. 2007 Aug 9;. PMID:17685615

Page seeded by OCA on Mon Nov 12 23:27:43 2007

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