Crystal Structure of the human BRPF1 bromodomain in complex with a histone H2AK5ac peptide

Structural insights into recognition of acetylated histone ligands by the BRPF1 bromodomain.

histone H2AK5ac peptide (UNP residues 2-13)

Bromodomain and PHD finger-containing protein 1, Protein Br140

GPLQLTPFLILLRKTLEQLQEKDTGNIFSEPVPLSEVPDYLDHIKKPMDFFTMKQNLEAYRYLNFDDFEEDFNLIVSNCL
KYNAKDTIFYRAAVRLREQGGAVLRQARRQAEKMGID

0.2 M NH4SO4, 0.1 M MES monohydrate, pH 6.5, 30% w/v polyethylene glycol monomethyl ether (PEG) 5000, 1% propylene glycol, VAPOR DIFFUSION, HANGING DROP, temperature 277K

Same protein complexed with the histone H4K12ac peptide

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

bromodomain-PHD finger protein 1 (BRPF1), histone acetyltransferase (HAT), monocytic leukemia zinc-finger (MOZ), epigenetics, chromatin reader, bromodomain, histone post-transcriptional modification (PTM) reader domain, acetyllysine, nucleus, Protein binding

QLTPFLILLRKTLEQLQEKDTGNIFSEPVPLSEVPDYLDHIKKPMDFFTMKQNLEAYRYLNFDDFEEDFNLIVSNCLKYN
AKDTIFYRAAVRLREQGGAVLRQARRQAEKMGID