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PDBsum entry 1fv5
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Transcription
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PDB id
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1fv5
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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 structures of two cchc zinc fingers from the fog family protein u-Shaped that mediate protein-Protein interactions.
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Authors
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C.K.Liew,
K.Kowalski,
A.H.Fox,
A.Newton,
B.K.Sharpe,
M.Crossley,
J.P.Mackay.
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Ref.
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Structure, 2000,
8,
1157-1166.
[DOI no: ]
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PubMed id
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Abstract
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BACKGROUND: Zinc finger domains have traditionally been regarded as
sequence-specific DNA binding motifs. However, recent evidence indicates that
many zinc fingers mediate specific protein-protein interactions. For instance,
several zinc fingers from FOG family proteins have been shown to interact with
the N-terminal zinc finger of GATA-1. RESULTS: We have used NMR spectroscopy to
determine the first structures of two FOG family zinc fingers that are involved
in protein-protein interactions: fingers 1 and 9 from U-shaped. These fingers
resemble classical TFIIIA-like zinc fingers, with the exception of an unusual
extended portion of the polypeptide backbone prior to the fourth zinc ligand.
[15N,(1)H]-HSQC titrations have been used to define the GATA binding surface of
USH-F1, and comparison with other FOG family proteins indicates that the
recognition mechanism is conserved across species. The surface of FOG-type
fingers that interacts with GATA-1 overlaps substantially with the surface
through which classical fingers typically recognize DNA. This suggests that
these fingers could not contact both GATA and DNA simultaneously. In addition,
results from NMR, gel filtration, and sedimentation equilibrium experiments
suggest that the interactions are of moderate affinity. CONCLUSIONS: Our results
demonstrate unequivocally that zinc fingers comprising the classical
betabetaalpha fold are capable of mediating specific contacts between proteins.
The existence of this alternative function has implications for the prediction
of protein function from sequence data and for the evolution of protein function.
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Figure 3.
Figure 3. Overlays of USH-F9 and the Sixth Finger from
ZFYUSH-F9 is shown in blue, and the sixth finger from ZFY [23]
is shown in red. The overlays are related by a 90° rotation
about a horizontal axis in the plane of the page. The
differences in side chain conformation in this region can be
clearly seen
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The above figure is
reprinted
by permission from Cell Press:
Structure
(2000,
8,
1157-1166)
copyright 2000.
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