› 2czy

Solution NMR

Solution structure of the NRSF/REST-mSin3B PAH1 complex

Released:
DOI: 10.2210/pdb2czy/pdb
PDB entry 2czy coloured by chain, ensemble of 20 models, front view.
PDB entry 2czy coloured by chain, ensemble of 20 models, side view.
PDB entry 2czy coloured by chain, ensemble of 20 models, top view.
Source organisms:
Primary publication:
The neural repressor NRSF/REST binds the PAH1 domain of the Sin3 corepressor by using its distinct short hydrophobic helix.
Nomura M, Uda-Tochio H, Murai K, Mori N, Nishimura Y
J Mol Biol 354 903-15 (2005)
PMID: 16288918

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171546 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Paired amphipathic helix protein Sin3b Chain: A
Molecule details ›
Chain: A
Length: 77 amino acids
Theoretical weight: 8.81 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q62141 (Residues: 31-107; Coverage: 7%)
Gene names: Kiaa0700, Sin3b
Sequence domains: Paired amphipathic helix repeat
Structure domains: Paired amphipathic helix
RE1-silencing transcription factor Chain: B
Molecule details ›
Chain: B
Length: 15 amino acids
Theoretical weight: 1.54 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q13127 (Residues: 43-57; Coverage: 1%)
Gene names: NRSF, REST, XBR

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

Quick links

Citations

11 review citations

Chromatin crosstalk in development and disease: lessons from REST.
Ooi et al. (2007)
10 more

14 mentions without citation

Co-repressor, co-activator and general transcription factor: the many faces of the Sin3 histone deacetylase (HDAC) complex.
Adams et al. (2018)
13 more