4YY4

Crystal structure of BRD9 Bromodomain bound to DMSO

Summary for 4YY4

• Entry DOI: 10.2210/pdb4yy4/pdb
• Related: 4YY6 4YYD 4YYG 4YYH 4YYI 4YYJ 4YYK 4YYM 4YYN
• Descriptor: Bromodomain-containing protein 9, DIMETHYL SULFOXIDE (3 entities in total)
• Functional Keywords: complex, protein binding
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 1
• Total formula weight: 12522.59

Authors

Tang, Y.,Bellon, S.,Cochran, A.G.,Poy, F. (deposition date: 2015-03-23, release date: 2015-09-16, Last modification date: 2023-09-27)

Primary citation

Flynn, E.M.,Huang, O.W.,Poy, F.,Oppikofer, M.,Bellon, S.F.,Tang, Y.,Cochran, A.G.
A Subset of Human Bromodomains Recognizes Butyryllysine and Crotonyllysine Histone Peptide Modifications.
Structure, 23:1801-1814, 2015

PubMed Abstract: Bromodomains are epigenetic readers that are recruited to acetyllysine residues in histone tails. Recent studies have identified non-acetyl acyllysine modifications, raising the possibility that these might be read by bromodomains. Profiling the nearly complete human bromodomain family revealed that while most human bromodomains bind only the shorter acetyl and propionyl marks, the bromodomains of BRD9, CECR2, and the second bromodomain of TAF1 also recognize the longer butyryl mark. In addition, the TAF1 second bromodomain is capable of binding crotonyl marks. None of the human bromodomains tested binds succinyl marks. We characterized structurally and biochemically the binding to different acyl groups, identifying bromodomain residues and structural attributes that contribute to specificity. These studies demonstrate a surprising degree of plasticity in some human bromodomains but no single factor controlling specificity across the family. The identification of candidate butyryl- and crotonyllysine readers supports the idea that these marks could have specific physiological functions.

PubMed: 26365797
DOI: 10.1016/j.str.2015.08.004

Experimental method

X-RAY DIFFRACTION (1.47 Å)