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PDBsum entry 4wn5

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protein ligands Protein-protein interface(s) links
Transcription PDB id
4wn5

 

 

 

 

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Contents
Protein chains
108 a.a.
Ligands
SO4 ×2
MVC ×2
P6G ×5
Waters ×295
PDB id:
4wn5
Name: Transcription
Title: Crystal structure of thE C-terminal per-arnt-sim (pasb) of human hif- 3alpha9 bound to 18:1-1-monoacylglycerol
Structure: Hypoxia-inducible factor 3-alpha. Chain: a, b. Fragment: unp residues 235-345. Synonym: hif3-alpha,basic-helix-loop-helix-pas protein mop7,class e basic helix-loop-helix protein 17,bhlhe17,hif3-alpha-1,inhibitory pas domain protein,ipas,member of pas protein 7,pas domain-containing protein 7. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: hif3a, bhlhe17, mop7, pasd7. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.15Å     R-factor:   0.123     R-free:   0.141
Authors: A.M.Fala,J.F.Oliveira,S.M.Dias,A.L.Ambrosio
Key ref: A.M.Fala et al. (2015). Unsaturated fatty acids as high-affinity ligands of the C-terminal Per-ARNT-Sim domain from the Hypoxia-inducible factor 3α. Sci Rep, 5, 12698. PubMed id: 26237540 DOI: 10.1038/srep12698
Date:
10-Oct-14     Release date:   05-Aug-15    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q9Y2N7  (HIF3A_HUMAN) -  Hypoxia-inducible factor 3-alpha from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
669 a.a.
108 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 

 
DOI no: 10.1038/srep12698 Sci Rep 5:12698 (2015)
PubMed id: 26237540  
 
 
Unsaturated fatty acids as high-affinity ligands of the C-terminal Per-ARNT-Sim domain from the Hypoxia-inducible factor 3α.
A.M.Fala, J.F.Oliveira, D.Adamoski, J.A.Aricetti, M.M.Dias, M.V.B.Dias, M.L.Sforça, P.S.Lopes-de-Oliveira, S.A.Rocco, C.Caldana, S.M.G.Dias, A.L.B.Ambrosio.
 
  ABSTRACT  
 
Hypoxia-inducible transcription factors (HIF) form heterodimeric complexes that mediate cell responses to hypoxia. The oxygen-dependent stability and activity of the HIF-α subunits is traditionally associated to post-translational modifications such as hydroxylation, acetylation, ubiquitination, and phosphorylation. Here we report novel evidence showing that unsaturated fatty acids are naturally occurring, non-covalent structural ligands of HIF-3α, thus providing the initial framework for exploring its exceptional role as a lipid sensor under hypoxia.
 

 

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