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PDBsum entry 2rje
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Transcription
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PDB id
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2rje
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References listed in PDB file
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Key reference
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Title
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L3mbtl1 recognition of mono- And dimethylated histones.
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Authors
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J.Min,
A.Allali-Hassani,
N.Nady,
C.Qi,
H.Ouyang,
Y.Liu,
F.Mackenzie,
M.Vedadi,
C.H.Arrowsmith.
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Ref.
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Nat Struct Biol, 2007,
14,
1229-1230.
[DOI no: ]
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PubMed id
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Abstract
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Crystal structures of the L3MBTL1 MBT repeats in complex with histone H4
peptides dimethylated on Lys20 (H4K20me2) show that only the second of the three
MBT repeats can bind mono- and dimethylated histone peptides. Its binding pocket
has similarities to that of 53BP1 and is able to recognize the degree of histone
lysine methylation. An unexpected mode of peptide-mediated dimerization suggests
a possible mechanism for chromatin compaction by L3MBTL1.
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Figure 1.
(a) Structure of 3MBT bound to an H4K20me2 peptide (residues
17–25). H4K20me2 peptide is shown in red and the
dimethyllysine is shown as a stick model. (b) Sequence alignment
of MBT2, MBT1 and MBT3. Red, identical; blue, conserved; dots,
lysine-binding pocket residues. (c) Superimposition of the three
MBT repeats in 3MBT. Residues forming the lysine-binding pocket
are shown as green sticks, and Phe256 from MBT1 and Arg467 from
MBT3 are colored pink and blue, respectively. H4K20me2 peptide
is shown as yellow sticks.
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Figure 2.
(a,b) 3MBT (a, green backbone) and 53BP1 (b, gray backbone).
Lysine-binding pocket residues and H4K20me2 peptide are shown as
stick models.
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The above figures are
reprinted
by permission from Macmillan Publishers Ltd:
Nat Struct Biol
(2007,
14,
1229-1230)
copyright 2007.
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