4QYD: Crystal Structure Of The Human Brpf1 Bromodomain In Complex With A Histone H4k12ac Peptide

Citation:
Abstract
Bromodomain-PHD finger protein 1 (BRPF1) is part of the MOZ HAT complex and contains a unique combination of domains typically found in chromatin-associated factors, which include plant homeodomain (PHD) fingers, a bromodomain and a proline-tryptophan-tryptophan-proline (PWWP) domain. Bromodomains are conserved structural motifs generally known to recognize acetylated histones, and the BRPF1 bromodomain preferentially selects for H2AK5ac, H4K12ac and H3K14ac. We solved the X-ray crystal structures of the BRPF1 bromodomain in complex with the H2AK5ac and H4K12ac histone peptides. Site-directed mutagenesis on residues in the BRPF1 bromodomain-binding pocket was carried out to investigate the contribution of specific amino acids on ligand binding. Our results provide critical insights into the molecular mechanism of ligand binding by the BRPF1 bromodomain, and reveal that ordered water molecules are an essential component driving ligand recognition.
PDB ID: 4QYDDownload
MMDB ID: 123452
PDB Deposition Date: 2014/7/24
Updated in MMDB: 2014/12
Experimental Method:
x-ray diffraction
Resolution: 1.94  Å
Source Organism:
Similar Structures:
Biological Unit for 4QYD: dimeric; determined by author and by software (PISA)
Molecular Components in 4QYD
Label Count Molecule
Proteins (2 molecules)
1
Peregrin(Gene symbol: BRPF1)
Molecule annotation
1
Histone H4(Gene symbol: HIST1H4I)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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