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PDBsum entry 2kis
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Transcription regulator
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PDB id
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2kis
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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 studies of ff domains of the transcription factor ca150 provide insights into the organization of ff domain tandem arrays.
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Authors
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J.M.Murphy,
D.F.Hansen,
S.Wiesner,
D.R.Muhandiram,
M.Borg,
M.J.Smith,
F.Sicheri,
L.E.Kay,
J.D.Forman-Kay,
T.Pawson.
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Ref.
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J Mol Biol, 2009,
393,
409-424.
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PubMed id
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Abstract
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FF domains are poorly understood protein interaction modules that are present
within eukaryotic transcription factors, such as CA150 (TCERG-1). The CA150 FF
domains have been shown to mediate interactions with the phosphorylated
C-terminal domain of RNA polymerase II (phosphoCTD) and a multitude of
transcription factors and RNA processing proteins, and may therefore have a
central role in organizing transcription. FF domains occur in tandem arrays of
up to six domains, although it is not known whether they adopt higher-order
structures. We have used the CA150 FF1+FF2 domains as a model system to examine
whether tandem FF domains form higher-order structures in solution using NMR
spectroscopy. In the solution structure of FF1 fused to the linker that joins
FF1 to FF2, we observed that the highly conserved linker peptide is ordered and
forms a helical extension of helix alpha3, suggesting that the interdomain
linker might have a role in orientating FF1 relative to FF2. However,
examination of the FF1+FF2 domains using relaxation NMR experiments revealed
that although these domains are not rigidly orientated relative to one another,
they do not tumble independently. Thus, the FF1+FF2 structure conforms to a
dumbbell-shape in solution, where the helical interdomain linker maintains
distance between the two dynamic FF domains without cementing their relative
orientations. This model for FF domain organization within tandem arrays
suggests a general mechanism by which individual FF domains can manoeuvre to
achieve optimal recognition of flexible binding partners, such as the
intrinsically-disordered phosphoCTD.
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