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PDBsum entry 4dos

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protein ligands links
Transcription PDB id
4dos

 

 

 

 

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Contents
Protein chains
242 a.a.
11 a.a.
Ligands
ASN-ALA-LEU-LEU-
ARG-TYR-LEU-LEU-
ASP-LYS
1PE ×3
PLC
Waters ×138
PDB id:
4dos
Name: Transcription
Title: Human nuclear receptor liver receptor homologue-1, lrh-1, bound to dlpc and a fragment of tif-2
Structure: Nuclear receptor subfamily 5 group a member 2. Chain: a. Fragment: ligand binding domain, unp residues 299-538. Synonym: alpha-1-fetoprotein transcription factor, b1-binding factor, hb1f, cyp7a promoter-binding factor, hepatocytic transcription factor, liver receptor homolog 1, lrh-1. Engineered: yes. Nuclear receptor coactivator 2. Chain: b, c.
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: b1f, cpf, ftf, lrh-1, nr5a2. Expressed in: escherichia coli. Expression_system_taxid: 469008. Synthetic: yes. Organism_taxid: 9606
Resolution:
2.00Å     R-factor:   0.191     R-free:   0.238
Authors: P.M.Musille,E.A.Ortlund
Key ref: P.M.Musille et al. (2012). Antidiabetic phospholipid-nuclear receptor complex reveals the mechanism for phospholipid-driven gene regulation. Nat Struct Biol, 19, 532-537. PubMed id: 22504882
Date:
10-Feb-12     Release date:   18-Apr-12    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
O00482  (NR5A2_HUMAN) -  Nuclear receptor subfamily 5 group A member 2 from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
541 a.a.
242 a.a.*
Protein chain
Pfam   ArchSchema ?
Q15596  (NCOA2_HUMAN) -  Nuclear receptor coactivator 2 from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1464 a.a.
11 a.a.
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: Chains A, C: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
Nat Struct Biol 19:532-537 (2012)
PubMed id: 22504882  
 
 
Antidiabetic phospholipid-nuclear receptor complex reveals the mechanism for phospholipid-driven gene regulation.
P.M.Musille, M.C.Pathak, J.L.Lauer, W.H.Hudson, P.R.Griffin, E.A.Ortlund.
 
  ABSTRACT  
 
No abstract given.

 

 

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