› 1u2n

Solution NMR

Structure CBP TAZ1 Domain

Released:
DOI: 10.2210/pdb1u2n/pdb
PDB entry 1u2n coloured by chain, ensemble of 20 models, front view.
PDB entry 1u2n coloured by chain, ensemble of 20 models, side view.
PDB entry 1u2n coloured by chain, ensemble of 20 models, top view.
Source organism: Mus musculus
Primary publication:
CBP/p300 TAZ1 domain forms a structured scaffold for ligand binding.
De Guzman RN, Wojciak JM, Martinez-Yamout MA, Dyson HJ, Wright PE
Biochemistry 44 490-7 (2005)
PMID: 15641773

Function and Biology Details

Reaction catalysed: 
Acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N(6)-acetyl-L-lysine
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155294 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone lysine acetyltransferase CREBBP Chain: A
Molecule details ›
Chain: A
Length: 100 amino acids
Theoretical weight: 11.32 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P45481 (Residues: 340-439; Coverage: 4%)
Gene names: Cbp, Crebbp
Sequence domains: TAZ zinc finger
Structure domains: TAZ domain

Ligands and Environments

1 bound ligand:
Ligand ZN 3 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: torsion angle dynamics by DYANA, simulated annealing and molecular dynamics by AMBER
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Transcriptional/epigenetic regulator CBP/p300 in tumorigenesis: structural and functional versatility in target recognition.
Wang et al. (2013)
1 more

7 mentions without citation

Modulation of epigenetic targets for anticancer therapy: clinicopathological relevance, structural data and drug discovery perspectives.
Andreoli et al. (2013)
6 more