› 2kby

Solution NMR

The Tetramerization Domain of Human p73

Released:
DOI: 10.2210/pdb2kby/pdb
PDB entry 2kby coloured by chain, ensemble of 20 models, front view.
PDB entry 2kby coloured by chain, ensemble of 20 models, side view.
PDB entry 2kby coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Conformational stability and activity of p73 require a second helix in the tetramerization domain.
Coutandin D, Löhr F, Niesen FH, Ikeya T, Weber TA, Schäfer B, Zielonka EM, Bullock AN, Yang A, Güntert P, Knapp S, McKeon F, Ou HD, Dötsch V
Cell Death Differ 16 1582-9 (2009)
PMID: 19763140

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tumor protein p73 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 50 amino acids
Theoretical weight: 6.03 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O15350 (Residues: 351-398; Coverage: 8%)
Gene names: P73, TP73
Sequence domains: P53 tetramerisation motif
Structure domains: p53-like tetramerisation domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: torsion angle dynamics
Expression system: Escherichia coli

Quick links

Citations

17 review citations

p63 and p73, the ancestors of p53.
Dötsch et al. (2010)
16 more

6 mentions without citation

Structural diversity of p63 and p73 isoforms.
Osterburg et al. (2022)
5 more