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Solution NMR

Solution structure of human PHF20 Tudor2 domain bound to a p53 segment containing a dimethyllysine analog p53K370me2

Released:
DOI: 10.2210/pdb2ldm/pdb
PDB entry 2ldm coloured by chain, ensemble of 20 models, front view.
PDB entry 2ldm coloured by chain, ensemble of 20 models, side view.
PDB entry 2ldm coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
PHF20 is an effector protein of p53 double lysine methylation that stabilizes and activates p53.
Cui G, Park S, Badeaux AI, Kim D, Lee J, Thompson JR, Yan F, Kaneko S, Yuan Z, Botuyan MV, Bedford MT, Cheng JQ, Mer G
Nat Struct Mol Biol 19 916-24 (2012)
PMID: 22864287

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-162886 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Uncharacterized protein Chain: A
Molecule details ›
Chain: A
Length: 81 amino acids
Theoretical weight: 9.07 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
Structure domains: SH3 type barrels.

Ligands and Environments

No bound ligands
1 modified residue:
Ligand M2L 1 x M2L

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 88%
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

20 review citations

Non-histone protein methylation as a regulator of cellular signalling and function.
Biggar et al. (2015)
19 more

3 mentions without citation

PHF20 Readers Link Methylation of Histone H3K4 and p53 with H4K16 Acetylation.
Klein et al. (2016)
2 more