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PDBsum entry 3lw2
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Hydrolase inhibitor
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PDB id
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3lw2
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Contents |
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* Residue conservation analysis
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PDB id:
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| Name: |
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Hydrolase inhibitor
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Title:
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Mouse plasminogen activator inhibitor-1 (pai-1)
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Structure:
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Plasminogen activator inhibitor 1. Chain: a. Fragment: pai-1. Synonym: pai-1, pai, endothelial plasminogen activator inhibitor. Engineered: yes
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Source:
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Mus musculus. Mouse. Organism_taxid: 10090. Gene: serpine1, mr1, pai1, planh1. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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1.93Å
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R-factor:
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0.183
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R-free:
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0.218
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Authors:
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M.Dewilde,B.Van De Craen,G.Compernolle,J.B.Madsen,S.V.Strelkov, A.Gils,P.J.Declerck
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Key ref:
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M.Dewilde
et al.
(2010).
Subtle structural differences between human and mouse PAI-1 reveal the basis for biochemical differences.
J Struct Biol,
171,
95.
PubMed id:
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Date:
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23-Feb-10
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Release date:
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07-Apr-10
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PROCHECK
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Headers
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References
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P22777
(PAI1_MOUSE) -
Plasminogen activator inhibitor 1 from Mus musculus
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Seq:
Struc:
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402 a.a.
365 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
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J Struct Biol
171:95
(2010)
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PubMed id:
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Subtle structural differences between human and mouse PAI-1 reveal the basis for biochemical differences.
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M.Dewilde,
B.Van De Craen,
G.Compernolle,
J.B.Madsen,
S.Strelkov,
A.Gils,
P.J.Declerck.
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ABSTRACT
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Plasminogen activator inhibitor-1 (PAI-1) is a serine protease inhibitor
(serpin) that plays an important role in cardiovascular disorders and tumor
development. The potential role of PAI-1 as a drug target has been evaluated in
various animal models (e.g. mouse and rat). Sensitivity to PAI-1 inhibitory
agents varied in different species. To date, absence of PAI-1 structures from
species other than human hampers efforts to reveal the molecular basis for the
observed species differences. Here we describe the structure of latent mouse
PAI-1. Comparison with available structures of human PAI-1 reveals (1) a
differential positioning of alpha-helix A; (2) differences in the gate region;
and (3) differences in the reactive center loop position. We demonstrate that
the optimal binding site of inhibitors may be dependent on the orthologs, and
our results affect strategies in the rational design of a pharmacologically
active PAI-1 inhibitor.
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Links
