1p0s
From Proteopedia
(New page: 200px<br /> <applet load="1p0s" size="450" color="white" frame="true" align="right" spinBox="true" caption="1p0s, resolution 2.80Å" /> '''Crystal Structure o...) |
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'''Crystal Structure of Blood Coagulation Factor Xa in Complex with Ecotin M84R'''<br /> | '''Crystal Structure of Blood Coagulation Factor Xa in Complex with Ecotin M84R'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
- | 1P0S is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MG and NA as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Coagulation_factor_Xa Coagulation factor Xa], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.6 3.4.21.6] Full crystallographic information is available from [http:// | + | 1P0S is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=NA:'>NA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Coagulation_factor_Xa Coagulation factor Xa], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.6 3.4.21.6] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P0S OCA]. |
==Reference== | ==Reference== | ||
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[[Category: serine protease inhibitor]] | [[Category: serine protease inhibitor]] | ||
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Revision as of 14:38, 15 February 2008
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Crystal Structure of Blood Coagulation Factor Xa in Complex with Ecotin M84R
Contents |
Overview
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.
Disease
Known disease associated with this structure: Factor X deficiency OMIM:[227600]
About this Structure
1P0S is a Protein complex structure of sequences from Escherichia coli and Homo sapiens with and as ligands. Active as Coagulation factor Xa, with EC number 3.4.21.6 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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