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PDBsum entry 6mlc
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PDB id:
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Transferase
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Title:
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Phd6 domain of mll3 in complex with histone h4
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Structure:
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Histone-lysine n-methyltransferase 2c. Chain: a, b, c, d. Fragment: phd-type 7 zinc finger, residues 1055-1144. Synonym: lysine n-methyltransferase 2c,homologous to alr protein, myeloid/lymphoid or mixed-lineage leukemia protein 3. Engineered: yes. Histone h4. Chain: e, f. Fragment: residues 2-21.
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: kmt2c, halr, kiaa1506, mll3. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Synthetic: yes. Organism_taxid: 9606
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Resolution:
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1.80Å
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R-factor:
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0.195
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R-free:
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0.216
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Authors:
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A.Dong,Y.Liu,S.Qin,M.Lei,C.Bountra,C.H.Arrowsmith,A.M.Edwards,J.Min, Structural Genomics Consortium (Sgc)
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Key ref:
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Y.Liu
et al.
(2019).
Structural insights into trans-histone regulation of H3K4 methylation by unique histone H4 binding of MLL3/4.
Nat Commun,
10,
36.
PubMed id:
DOI:
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Date:
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27-Sep-18
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Release date:
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24-Oct-18
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PROCHECK
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Headers
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References
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Q8NEZ4
(KMT2C_HUMAN) -
Histone-lysine N-methyltransferase 2C from Homo sapiens
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Seq:
Struc:
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4911 a.a.
85 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
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Enzyme class:
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E.C.2.1.1.364
- [histone H3]-lysine(4) N-methyltransferase.
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Reaction:
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L-lysyl4-[histone H3] + S-adenosyl-L-methionine = N6-methyl-L- lysyl4-[histone H3] + S-adenosyl-L-homocysteine + H+
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L-lysyl(4)-[histone H3]
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+
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S-adenosyl-L-methionine
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=
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N(6)-methyl-L- lysyl(4)-[histone H3]
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+
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S-adenosyl-L-homocysteine
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+
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H(+)
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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DOI no:
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Nat Commun
10:36
(2019)
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PubMed id:
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Structural insights into trans-histone regulation of H3K4 methylation by unique histone H4 binding of MLL3/4.
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Y.Liu,
S.Qin,
T.Y.Chen,
M.Lei,
S.S.Dhar,
J.C.Ho,
A.Dong,
P.Loppnau,
Y.Li,
M.G.Lee,
J.Min.
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ABSTRACT
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MLL3 and MLL4 are two closely related members of the SET1/MLL family of histone
H3K4 methyltransferases and are responsible for monomethylating histone H3K4 on
enhancers, which are essential in regulating cell-type-specific gene expression.
Mutations of MLL3 or MLL4 have been reported in different types of cancer.
Recently, the PHD domains of MLL3/4 have been reported to recruit the MLL3/4
complexes to their target genes by binding to histone H4 during the NT2/D1 stem
cell differentiation. Here we show that an extended PHD domain
(ePHD6) involving the sixth PHD domain and its preceding zinc finger
in MLL3 and MLL4 specifically recognizes an H4H18-containing histone H4 fragment
and that modifications of residues surrounding H4H18 modulate H4 binding to
MLL3/4. Our in vitro methyltransferase assays and cellular experiments further
reveal that the interaction between ePHD6 of MLL3/4 and histone H4 is
required for their nucleosomal methylation activity and MLL4-mediated neuronal
differentiation of NT2/D1 cells.
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