› 2rvn

Solution NMR

Solution structure of the chromodomain of HP1a with the phosphorylated N-terminal tail complexed with H3K9me3 peptide

Released:
DOI: 10.2210/pdb2rvn/pdb
PDB entry 2rvn coloured by chain, ensemble of 20 models, front view.
PDB entry 2rvn coloured by chain, ensemble of 20 models, side view.
PDB entry 2rvn coloured by chain, ensemble of 20 models, top view.
Source organism: Mus musculus
Primary publication:
Extended string-like binding of the phosphorylated HP1α N-terminal tail to the lysine 9-methylated histone H3 tail.
Shimojo H, Kawaguchi A, Oda T, Hashiguchi N, Omori S, Moritsugu K, Kidera A, Hiragami-Hamada K, Nakayama J, Sato M, Nishimura Y
Sci Rep 6 22527 (2016)
PMID: 26934956

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-160875 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Chromobox protein homolog 5 Chain: A
Molecule details ›
Chain: A
Length: 83 amino acids
Theoretical weight: 10.17 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q61686 (Residues: 1-80; Coverage: 42%)
Gene names: Cbx5, Hp1a
Sequence domains: Chromo (CHRromatin Organisation MOdifier) domain
Histone H3.3 Chain: B
Molecule details ›
Chain: B
Length: 18 amino acids
Theoretical weight: 2.03 KDa
Source organism: Mus musculus
Expression system: Not provided
UniProt:
  • Canonical: P84244 (Residues: 2-18; Coverage: 13%)
Gene names: H3-3a, H3-3b, H3.3a, H3.3b, H3f3a, H3f3b

Ligands and Environments

No bound ligands
2 modified residues:
Ligand SEP 4 x SEP
Ligand M3L 1 x M3L

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 90%
Refinement method: torsion angle dynamics
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

5 review citations

Application of NMR to studies of intrinsically disordered proteins.
Gibbs et al. (2017)
4 more

1 mention without citation

Extended string-like binding of the phosphorylated HP1α N-terminal tail to the lysine 9-methylated histone H3 tail.
Shimojo et al. (2016)