› 2agh

Solution NMR

Structural basis for cooperative transcription factor binding to the CBP coactivator

Released:
DOI: 10.2210/pdb2agh/pdb
PDB entry 2agh coloured by chain, ensemble of 20 models, front view.
PDB entry 2agh coloured by chain, ensemble of 20 models, side view.
PDB entry 2agh coloured by chain, ensemble of 20 models, top view.
Source organisms:
Primary publication:
Structural basis for cooperative transcription factor binding to the CBP coactivator.
De Guzman RN, Goto NK, Dyson HJ, Wright PE
J Mol Biol 355 1005-13 (2006)
PMID: 16253272

Function and Biology Details

Reactions catalysed: 
Acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N(6)-acetyl-L-lysine
S-adenosyl-L-methionine + a [histone H3]-L-lysine(4) = S-adenosyl-L-homocysteine + a [histone H3]-N(6)-methyl-L-lysine(4)
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-139293 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Transcriptional activator Myb Chain: A
Molecule details ›
Chain: A
Length: 25 amino acids
Theoretical weight: 2.95 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P06876 (Residues: 291-315; Coverage: 4%)
Gene name: Myb
Sequence domains: LMSTEN motif
Histone lysine acetyltransferase CREBBP Chain: B
Molecule details ›
Chain: B
Length: 87 amino acids
Theoretical weight: 10.35 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P45481 (Residues: 586-672; Coverage: 4%)
Gene names: Cbp, Crebbp
Sequence domains: KIX domain
Structure domains: Coactivator CBP, KIX domain
MLL cleavage product C180 Chain: C
Molecule details ›
Chain: C
Length: 31 amino acids
Theoretical weight: 3.31 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q03164 (Residues: 2839-2869; Coverage: 1%)
Gene names: ALL1, CXXC7, HRX, HTRX, KMT2A, MLL, MLL1, TRX1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

19 review citations

Linking folding and binding.
Wright et al. (2009)
18 more

44 mentions without citation

The origin of allosteric functional modulation: multiple pre-existing pathways.
del Sol et al. (2009)
43 more