1hce

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==STRUCTURE OF HISACTOPHILIN IS SIMILAR TO INTERLEUKIN-1 BETA AND FIBROBLAST GROWTH FACTOR==
==STRUCTURE OF HISACTOPHILIN IS SIMILAR TO INTERLEUKIN-1 BETA AND FIBROBLAST GROWTH FACTOR==
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<StructureSection load='1hce' size='340' side='right' caption='[[1hce]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>
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<StructureSection load='1hce' size='340' side='right'caption='[[1hce]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1hce]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HCE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HCE FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1hce]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HCE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HCE FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1hcd|1hcd]]</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hce FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hce OCA], [http://pdbe.org/1hce PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hce RCSB], [http://www.ebi.ac.uk/pdbsum/1hce PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1hce ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1hce FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hce OCA], [https://pdbe.org/1hce PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hce RCSB], [https://www.ebi.ac.uk/pdbsum/1hce PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hce ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/HATA_DICDI HATA_DICDI]] May act as an intracellular pH sensor that links chemotactic signals to responses in the microfilament system of the cells by nucleating actin polymerization or stabilizing the filaments.
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[https://www.uniprot.org/uniprot/HATA_DICDI HATA_DICDI] May act as an intracellular pH sensor that links chemotactic signals to responses in the microfilament system of the cells by nucleating actin polymerization or stabilizing the filaments.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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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<ref>PMID:1436061</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1hce" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Gondol, D]]
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[[Category: Dictyostelium discoideum]]
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[[Category: Habazettl, J]]
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[[Category: Large Structures]]
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[[Category: Holak, T A]]
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[[Category: Gondol D]]
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[[Category: Otlewski, J]]
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[[Category: Habazettl J]]
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[[Category: Schleicher, M]]
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[[Category: Holak TA]]
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[[Category: Wiltscheck, R]]
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[[Category: Otlewski J]]
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[[Category: Actin binding]]
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[[Category: Schleicher M]]
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[[Category: Wiltscheck R]]

Current revision

STRUCTURE OF HISACTOPHILIN IS SIMILAR TO INTERLEUKIN-1 BETA AND FIBROBLAST GROWTH FACTOR

PDB ID 1hce

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