› 1pou

Solution NMR

THE SOLUTION STRUCTURE OF THE OCT-1 POU-SPECIFIC DOMAIN REVEALS A STRIKING SIMILARITY TO THE BACTERIOPHAGE LAMBDA REPRESSOR DNA-BINDING DOMAIN

Released:
DOI: 10.2210/pdb1pou/pdb
PDB entry 1pou coloured by chain, ensemble of 20 models, front view.
PDB entry 1pou coloured by chain, ensemble of 20 models, side view.
PDB entry 1pou coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
The solution structure of the Oct-1 POU-specific domain reveals a striking similarity to the bacteriophage lambda repressor DNA-binding domain.
Assa-Munt N, Mortishire-Smith RJ, Aurora R, Herr W, Wright PE
Cell 73 193-205 (1993)
PMID: 8462099

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147106 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
POU domain, class 2, transcription factor 1 Chain: A
Molecule details ›
Chain: A
Length: 71 amino acids
Theoretical weight: 8.23 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P14859 (Residues: 284-354; Coverage: 10%)
Gene names: OCT1, OTF1, POU2F1
Sequence domains: Pou domain - N-terminal to homeobox domain
Structure domains: lambda repressor-like DNA-binding domains

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Expression system: Not provided

Quick links

Citations

12 review citations

The virtuoso of versatility: POU proteins that flex to fit.
Phillips et al. (2000)
11 more

15 mentions without citation

Modification and optimization of the united-residue (UNRES) potential energy function for canonical simulations. I. Temperature dependence of the effective energy function and tests of the optimization method with single training proteins.
Liwo et al. (2007)
14 more