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PDBsum entry 4qyd
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Protein binding
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PDB id
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4qyd
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References listed in PDB file
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Key reference
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Title
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Structural insights into recognition of acetylated histone ligands by the brpf1 bromodomain.
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Authors
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M.Y.Lubula,
B.E.Eckenroth,
S.Carlson,
A.Poplawski,
M.Chruszcz,
K.C.Glass.
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Ref.
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Febs Lett, 2014,
588,
3844-3854.
[DOI no: ]
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PubMed id
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Abstract
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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.
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