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PDBsum entry 4z4p
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References listed in PDB file
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Key reference
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Title
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Evolving catalytic properties of the mll family set domain.
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Authors
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Y.Zhang,
A.Mittal,
J.Reid,
S.Reich,
S.J.Gamblin,
J.R.Wilson.
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Ref.
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Structure, 2015,
23,
1921-1933.
[DOI no: ]
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PubMed id
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Abstract
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Methylation of histone H3 lysine-4 is a hallmark of chromatin associated with
active gene expression. The activity of H3K4-specific modification enzymes, in
higher eukaryotes the MLL (or KMT2) family, is tightly regulated. The MLL family
has six members, each with a specialized function. All contain a catalytic SET
domain that associates with a core multiprotein complex for activation. These
SET domains segregate into three classes that correlate with the arrangement of
targeting domains that populate the rest of the protein. Here we show that,
unlike MLL1, the MLL4 SET domain retains significant activity without the core
complex. We also present the crystal structure of an inactive MLL4-tagged SET
domain construct and describe conformational changes that account for MLL4
intrinsic activity. Finally, our structure explains how the MLL SET domains are
able to add multiple methyl groups to the target lysine, despite having the
sequence characteristics of a classical monomethylase.
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