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PDBsum entry 3f70
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Transcription regulator
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PDB id
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3f70
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References listed in PDB file
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Key reference
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Title
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Methylation-State-Specific recognition of histones by the mbt repeat protein l3mbtl2.
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Authors
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Y.Guo,
N.Nady,
C.Qi,
A.Allali-Hassani,
H.Zhu,
P.Pan,
M.A.Adams-Cioaba,
M.F.Amaya,
A.Dong,
M.Vedadi,
M.Schapira,
R.J.Read,
C.H.Arrowsmith,
J.Min.
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Ref.
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Nucleic Acids Res, 2009,
37,
2204-2210.
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PubMed id
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Abstract
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The MBT repeat has been recently identified as a key domain capable of
methyl-lysine histone recognition. Functional work has pointed to a role for MBT
domain-containing proteins in transcriptional repression of developmental
control genes such as Hox genes. In this study, L3MBTL2, a human homolog of
Drosophila Sfmbt critical for Hox gene silencing, is demonstrated to
preferentially recognize lower methylation states of several histone-derived
peptides through its fourth MBT repeat. High-resolution crystallographic
analysis of the four MBT repeats of this protein reveals its unique asymmetric
rhomboid architecture, as well as binding mechanism, which preclude the
interaction of the first three MBT repeats with methylated peptides. Structural
elucidation of an L3MBTL2-H4K20me1 complex and comparison with other MBT-histone
peptide complexes also suggests that an absence of distinct surface contours
surrounding the methyl-lysine-binding pocket may underlie the lack of sequence
specificity observed for members of this protein family.
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