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PDBsum entry 2v0e
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References listed in PDB file
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Key reference
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Title
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Solution structure of the brk domains from chd7.
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Authors
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M.D.Allen,
T.L.Religa,
S.M.Freund,
M.Bycroft.
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Ref.
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J Mol Biol, 2007,
371,
1135-1140.
[DOI no: ]
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PubMed id
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Abstract
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CHD7 is a member of the chromodomain helicase DNA binding domain (CHD) family of
ATP-dependent chromatin remodelling enzymes. It is mutated in CHARGE syndrome, a
multiple congenital anomaly condition. CHD7 is one of a subset of CHD proteins,
unique to metazoans that contain the BRK domain, a protein module also found in
the Brahma/BRG1 family of helicases. We describe here the NMR solution structure
of the two BRK domains of CHD7. Each domain has a compact betabetaalphabeta
fold. The second domain has a C-terminal extension consisting of two additional
helices. The structure differs from those of other domains present in
chromatin-associated proteins.
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Figure 3.
Figure 3. CTCF binding. A GST fusion protein of the zinc
finger domains of human CTCF (lane 3) bound to glutathione beads
was incubated with the BRK domains of CHD7. After repeated
washing steps, binding of the BRK domains was analysed by
SDS–PAGE followed by Coomassie staining of the gel (lane 4).
GST served as a negative control (lanes 5 and 6). For
comparison, the BRK input is shown in lane 1. The BRK domains
did not bind to glutathione beads (lane 2).
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The above figure is
reprinted
by permission from Elsevier:
J Mol Biol
(2007,
371,
1135-1140)
copyright 2007.
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