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PDBsum entry 1hcd
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Actin binding
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PDB id
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1hcd
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References listed in PDB file
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Key reference
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Title
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Structure of hisactophilin is similar to interleukin-1 beta and fibroblast growth factor.
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Authors
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J.Habazettl,
D.Gondol,
R.Wiltscheck,
J.Otlewski,
M.Schleicher,
T.A.Holak.
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Ref.
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Nature, 1992,
359,
855-858.
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PubMed id
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Abstract
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The fast reaction of the actin-based cytoskeleton in motile cells after
stimulation with a chemoattractant requires a signal-transduction chain that
creates a very specific environment at distinct regions beneath the plasma
membrane. Dictyostelium hisactophilin, a unique actin-binding protein, is a
submembranous pH sensor that signals slight changes of the H+ concentration to
actin by inducing actin polymerization and binding to microfilaments only at pH
values below seven. It has a relative molecular mass of 13.5K and its most
unusual feature is the presence of 31 histidine residues among its total of 118
amino acids. The transduction of an external signal from the plasma membrane to
the cytoskeleton is poorly understood. Here we report the protein's structure in
solution determined by nuclear magnetic resonance spectroscopy. The nuclear
Overhauser effect intensities of the three-dimensional nuclear Overhauser
spectra were used directly in the calculations. The overall folding of
histactophilin is similar to that of interleukin-1 beta and fibroblast growth
factor, but the primary amino-acid sequence of hisactophilin is unrelated to
these two proteins.
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Secondary reference #1
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Title
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Homonuclear three-Dimensional noe-Noe nuclear magnetic resonance/spectra for structure determination of proteins in solution.
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Authors
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J.Habazettl,
M.Schleicher,
J.Otlewski,
T.A.Holak.
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Ref.
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J Mol Biol, 1992,
228,
156-169.
[DOI no: ]
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PubMed id
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Figure 3.
Figure 3. Upper (horizontal lines) error bounds A, and
lower (vertical lins) error bounds A, in the rxperiment,al
intensity plotted against the intensity I$.
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Figure 9.
Figure 9. Average pairwisc atomir r.m.s. differences
among the hisactophilin structures. l represents t,hr
residues that are involved in /?-sheet's; 0 represents
residues of turns and loops; 1 shows the stndard devia-
tions. The superposition of ,he strurturrs wsas as in Pip. 8.
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The above figures are
reproduced from the cited reference
with permission from Elsevier
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