› 2lvm

Solution NMR

Solution structure of human 53BP1 tandem Tudor domains in complex with a histone H4K20me2 peptide

Released:
DOI: 10.2210/pdb2lvm/pdb
PDB entry 2lvm coloured by chain, ensemble of 20 models, front view.
PDB entry 2lvm coloured by chain, ensemble of 20 models, side view.
PDB entry 2lvm coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Acetylation limits 53BP1 association with damaged chromatin to promote homologous recombination.
Tang J, Cho NW, Cui G, Manion EM, Shanbhag NM, Botuyan MV, Mer G, Greenberg RA
Nat Struct Mol Biol 20 317-25 (2013)
PMID: 23377543

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158678 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
TP53-binding protein 1 Chain: A
Molecule details ›
Chain: A
Length: 123 amino acids
Theoretical weight: 13.94 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q12888 (Residues: 1484-1603; Coverage: 6%)
Gene name: TP53BP1
Sequence domains: Tumour suppressor p53-binding protein-1 Tudor
Structure domains:
Histone H4 Chain: B
Molecule details ›
Chain: B
Length: 14 amino acids
Theoretical weight: 1.72 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P62805 (Residues: 15-28; Coverage: 14%)
Gene names: H4-16, H4/A, H4/B, H4/C, H4/D, H4/E, H4/G, H4/H, H4/I, H4/J, H4/K, H4/M, H4/N, H4/O, H4C1, H4C11, H4C12, H4C13, H4C14, H4C15, H4C16, H4C2, H4C3, H4C4, H4C5, H4C6, H4C8, H4C9, H4F2, H4FA, H4FB, H4FC, H4FD, H4FE, H4FG, H4FH, H4FI, H4FJ, H4FK, H4FM, H4FN, H4FO, HIST1H4A, HIST1H4B, HIST1H4C, HIST1H4D, HIST1H4E, HIST1H4F, HIST1H4H, HIST1H4I, HIST1H4J, HIST1H4K, HIST1H4L, HIST2H4, HIST2H4A, HIST2H4B, HIST4H4

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 91%
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

108 review citations

Double-strand break repair: 53BP1 comes into focus.
Panier et al. (2014)
107 more

9 mentions without citation

Tudor: a versatile family of histone methylation 'readers'.
Lu et al. (2013)
8 more