› 2ly4

Solution NMR

HMGB1-facilitated p53 DNA binding occurs via HMG-box/p53 transactivation domain interaction and is regulated by the acidic tail

Released:
DOI: 10.2210/pdb2ly4/pdb
PDB entry 2ly4 coloured by chain, ensemble of 10 models, front view.
PDB entry 2ly4 coloured by chain, ensemble of 10 models, side view.
PDB entry 2ly4 coloured by chain, ensemble of 10 models, top view.
Source organism: Homo sapiens
Primary publication:
HMGB1-Facilitated p53 DNA Binding Occurs via HMG-Box/p53 Transactivation Domain Interaction, Regulated by the Acidic Tail.
Rowell JP, Simpson KL, Stott K, Watson M, Thomas JO
Structure (2012)
PMID: 23063560

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138107 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
High mobility group protein B1 Chain: A
Molecule details ›
Chain: A
Length: 83 amino acids
Theoretical weight: 9.71 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P09429 (Residues: 2-84; Coverage: 39%)
Gene names: HMG1, HMGB1
Sequence domains: HMG-box domain
Structure domains: High mobility group box domain
Cellular tumor antigen p53 Chain: B
Molecule details ›
Chain: B
Length: 93 amino acids
Theoretical weight: 9.98 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P04637 (Residues: 1-93; Coverage: 24%)
Gene names: P53, TP53
Sequence domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 92%
Refinement method: DGSA-distance geometry simulated annealing
Expression system: Escherichia coli

Quick links

Citations

26 review citations

HMGB1 in health and disease.
Kang et al. (2014)
25 more

20 mentions without citation

Features of molecular recognition of intrinsically disordered proteins via coupled folding and binding.
Yang et al. (2019)
19 more