1hce
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(New page: 200px<br /><applet load="1hce" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hce" /> '''STRUCTURE OF HISACTOPHILIN IS SIMILAR TO INT...)
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Revision as of 14:23, 20 November 2007
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STRUCTURE OF HISACTOPHILIN IS SIMILAR TO INTERLEUKIN-1 BETA AND FIBROBLAST GROWTH FACTOR
Overview
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.
About this Structure
1HCE is a Single protein structure of sequence from Dictyostelium discoideum. Full crystallographic information is available from OCA.
Reference
Structure of hisactophilin is similar to interleukin-1 beta and fibroblast growth factor., Habazettl J, Gondol D, Wiltscheck R, Otlewski J, Schleicher M, Holak TA, Nature. 1992 Oct 29;359(6398):855-8. PMID:1436061
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