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PDBsum entry 3eox

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protein links
Blood clotting PDB id
3eox
Jmol PyMol
Contents
Protein chain
370 a.a. *
Waters ×123
* Residue conservation analysis
PDB id:
3eox
Name: Blood clotting
Title: High quality structure of cleaved pai-1-stab
Structure: Plasminogen activator inhibitor 1. Chain: a. Fragment: pai-1. Synonym: pai-1, pai, endothelial plasminogen activator inhi engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: serpine1, pai1, planh1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.61Å     R-factor:   0.204     R-free:   0.256
Authors: M.Dewilde,P.J.Declerck,A.Rabijns,S.V.Strelkov
Key ref: M.Dewilde et al. (2009). High quality structure of cleaved PAI-1-stab. J Struct Biol, 165, 126-132. PubMed id: 19059484
Date:
29-Sep-08     Release date:   17-Feb-09    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P05121  (PAI1_HUMAN) -  Plasminogen activator inhibitor 1
Seq:
Struc:
402 a.a.
370 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 5 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   6 terms 
  Biological process     positive regulation of leukotriene production involved in inflammatory response   30 terms 
  Biochemical function     protein binding     5 terms  

 

 
J Struct Biol 165:126-132 (2009)
PubMed id: 19059484  
 
 
High quality structure of cleaved PAI-1-stab.
M.Dewilde, S.V.Strelkov, A.Rabijns, P.J.Declerck.
 
  ABSTRACT  
 
Here we report the crystal structure of a stablilized plasminogen activator inhibitor-1 variant (PAI-1-N150H-K154T-Q301P-Q319L-M354I (PAI-1-stab)) that shows a cleavage within the reactive centre loop. The new structure is of superior quality compared to the previously determined structure of the cleaved PAI-1-A335P mutant. We present a detailed comparison of the two structures and also compare them with the structure of the active PAI-1-stab. The structural data give important insights into the working mechanism of PAI-1 and also explain the role of various stabilizing mutations.
 

 

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