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PDBsum entry 2grc
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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 ramification for acetyl-Lysine recognition by the bromodomain of human brg1 protein, A central atpase of the swi/snf remodeling complex.
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Authors
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M.Singh,
G.M.Popowicz,
M.Krajewski,
T.A.Holak.
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Ref.
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Chembiochem, 2007,
8,
1308-1316.
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PubMed id
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Abstract
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Bromodomains represent an extensive family of evolutionarily conserved domains
that are found in many chromatin-associated proteins such as histone
acetyltransferases (HAT) and subunits of ATP-dependent chromatin-remodeling
complexes. These domains are associated with acetylated lysine residues that
bind both in vivo and in vitro; for example, they bind to the N-acetylated
lysines of the histone tail of nucleosomes. In this report, we determined the
structure of the bromodomain from human brahma-related gene 1 (BRG1) protein, a
subunit of an ATP-dependent switching/sucrose nonfermenting (SWI/SNF) remodeling
complex, and have also characterized its in vitro interaction with N-acetylated
lysine peptides from histones. In addition to a typical all-alpha-helical fold
that was observed in the bromodomains, we observed for the first time a small
beta-sheet in the ZA loop region of the BRG1 protein. The BRG1 bromodomain
exhibited binding, albeit weak, to acetylated peptides that were derived from
histones H3 and H4. We have compared the acetyl-lysine binding sites of BRG1
bromodomain with the yGCN5 (general control of amino acid biosynthesis). By
modeling the acetylated-lysine peptide into the BRG1 bromodomain structure, we
were able to explain the weak binding of acetylated-lysine peptides to this
bromodomain.
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