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PDBsum entry 2qxv
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Gene regulation
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PDB id
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2qxv
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References listed in PDB file
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Key reference
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Title
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Structural basis of ezh2 recognition by eed.
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Authors
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Z.Han,
X.Xing,
M.Hu,
Y.Zhang,
P.Liu,
J.Chai.
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Ref.
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Structure, 2007,
15,
1306-1315.
[DOI no: ]
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PubMed id
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Abstract
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The WD-repeat domain is a highly conserved recognition module in eukaryotes
involved in diverse cellular processes. It is still not well understood how the
bottom of a WD-repeat domain recognizes its binding partners. The
WD-repeat-containing protein EED is one component of the PRC2 complex that
possesses histone methyltransferase activity required for gene repression. Here
we report the crystal structure of EED in complex with a 30 residue peptide from
EZH2. The structure reveals that the peptide binds to the bottom of the
WD-repeat domain of EED. The structural determinants of EZH2-EED interaction are
present not only in EZH2 and EZH1 but also in its Drosophila homolog E(Z),
suggesting that the recognition of ESC by E(Z) in Drosophila employs similar
structural motifs. Structure-based mutagenesis identified critical residues from
both EED and EZH2 for their interaction. The structure presented here may
provide a template for understanding of how WD-repeat proteins recognize their
interacting proteins.
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Figure 3.
Figure 3. EBD Binds to a Well-Defined Groove at the Bottom of
EED
(A) A schematic representation of EED and the
EED-binding domain in EZH2 (EBD) (residues 39–68). EED and EBD
are shown in cyan and orange, respectively.
(B)
Electrostatic complementarity between EED and EBD. Both EED and
EBD are represented in electrostatic surface. The positive,
negative, and neutral surfaces are colored in blue, red, and
white, respectively. To distinguish between EED and EBD, EBD is
also shown as a cartoon (cyan).
(C) Shape complementarity
between EED and EBD. EED and EBD are represented in mesh and
surface, respectively.
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Figure 5.
Figure 5. Structural Comparison of the EED-EBD Complex and
Gβγ Dimer
Superposition of the EED-EBD complex and Gβγ
dimer (Protein Data Bank ID code: 1TBG2) is viewed from two
different angles. EED, EBD, Gβ, and Gγ are colored in orange,
cyan, magenta, and light pink, respectively. The two labeled
residues shown in stick form are from EBD (marine) and Gγ
(slate).
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The above figures are
reprinted
by permission from Cell Press:
Structure
(2007,
15,
1306-1315)
copyright 2007.
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