1p0s

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{{STRUCTURE_1p0s| PDB=1p0s | SCENE= }}
{{STRUCTURE_1p0s| PDB=1p0s | SCENE= }}
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'''Crystal Structure of Blood Coagulation Factor Xa in Complex with Ecotin M84R'''
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===Crystal Structure of Blood Coagulation Factor Xa in Complex with Ecotin M84R===
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==Overview==
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The serine protease factor Xa (FXa) is inhibited by ecotin with picomolar affinity. The structure of the tetrameric complex of ecotin variant M84R (M84R) with FXa has been determined to 2.8 A. Substrate directed induced fit of the binding interactions at the S2 and S4 pockets modulates the discrimination of the protease. Specifically, the Tyr at position 99 of FXa changes its conformation with respect to incoming ligand, changing the size of the S2 and S4 pockets. The role of residue 192 in substrate and inhibitor recognition is also examined. Gln 192 from FXa forms a hydrogen bond with the P2 carbonyl group of ecotin. This confirms previous biochemical and structural analyses on thrombin and activated protein C, which suggested that residue 192 may play a more general role in mediating the interactions between coagulation proteases and their inhibitors. The structure of ecotin M84R-FXa (M84R-FXa) also reveals the structure of the Gla domain in the presence of Mg(2+). The first 11 residues of the domain assume a novel conformation and likely represent an intermediate folding state of the domain.
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{{ABSTRACT_PUBMED_12834348}}
==About this Structure==
==About this Structure==
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[[Category: Serine protease]]
[[Category: Serine protease]]
[[Category: Serine protease inhibitor]]
[[Category: Serine protease inhibitor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:32:24 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 16:29:40 2008''

Revision as of 13:29, 27 July 2008

Image:1p0s.png

Template:STRUCTURE 1p0s

Crystal Structure of Blood Coagulation Factor Xa in Complex with Ecotin M84R

Template:ABSTRACT PUBMED 12834348

About this Structure

1P0S is a Protein complex structure of sequences from Escherichia coli and Homo sapiens. Full crystallographic information is available from OCA.

Reference

The extended interactions and Gla domain of blood coagulation factor Xa., Wang SX, Hur E, Sousa CA, Brinen L, Slivka EJ, Fletterick RJ, Biochemistry. 2003 Jul 8;42(26):7959-66. PMID:12834348

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