Co-crystal Structure

Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.

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

The pathogenic sequelae of BRCA1 mutation in human and mouse cells are mitigated by concomitant deletion of 53BP1, which binds histone H4 dimethylated at Lys20 (H4K20me2) to promote nonhomologous end joining, suggesting that a balance between BRCA1 and 53BP1 regulates DNA double strand-break (DSB) repair mechanism choice. Here we document that acetylation is a key determinant of this balance. TIP60 ... [more]

Nat. Struct. Mol. Biol. Mar. 01, 2013; 20(3);317-25 [Pubmed: 23377543]

Throughput

  • Low Throughput

Additional Notes

  • NMR Spectroscopy

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
TP53BP1 HIST2H4A
Protein-peptide
Protein-peptide

An interaction is detected between a protein and a peptide derived from an interaction partner. This includes phage display experiments.

Low-BioGRID
-

Curated By

  • BioGRID