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PDBsum entry 2f5k
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Gene regulation
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PDB id
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2f5k
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References listed in PDB file
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Key reference
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Title
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Structure of human mrg15 chromo domain and its binding to lys36-Methylated histone h3.
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Authors
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P.Zhang,
J.Du,
B.Sun,
X.Dong,
G.Xu,
J.Zhou,
Q.Huang,
Q.Liu,
Q.Hao,
J.Ding.
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Ref.
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Nucleic Acids Res, 2006,
34,
6621-6628.
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PubMed id
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Abstract
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Human MRG15 is a transcription factor that plays a vital role in embryonic
development, cell proliferation and cellular senescence. It comprises a putative
chromo domain in the N-terminal part that has been shown to participate in
chromatin remodeling and transcription regulation. We report here the crystal
structure of human MRG15 chromo domain at 2.2 A resolution. The MRG15 chromo
domain consists of a beta-barrel and a long alpha-helix and assumes a structure
more similar to the Drosophila MOF chromo barrel domain than the typical HP1/Pc
chromo domains. The beta-barrel core contains a hydrophobic pocket formed by
three conserved aromatic residues Tyr26, Tyr46 and Trp49 as a potential binding
site for a modified residue of histone tail. However, the binding groove for the
histone tail seen in the HP1/Pc chromo domains is pre-occupied by an extra
beta-strand. In vitro binding assay results indicate that the MRG15 chromo
domain can bind to methylated Lys36, but not methylated Lys4, Lys9 and Lys27 of
histone H3. These data together suggest that the MRG15 chromo domain may
function as an adaptor module which can bind to a modified histone H3 in a mode
different from that of the HP1/Pc chromo domains.
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