4YYH: Crystal Structure Of Brd9 Bromodomain Bound To A Crotonyllysine Peptide

Citation:
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.
PDB ID: 4YYHDownload
MMDB ID: 132641
PDB Deposition Date: 2015/3/23
Updated in MMDB: 2015/11
Experimental Method:
x-ray diffraction
Resolution: 1.74  Å
Source Organism:
Similar Structures:
Biological Unit for 4YYH: dimeric; determined by author
Molecular Components in 4YYH
Label Count Molecule
Proteins (2 molecules)
1
Bromodomain-containing Protein 9(Gene symbol: BRD9)
Molecule annotation
1
Histone H4(Gene symbol: HIST1H4I)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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