1ak6

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[[Image:1ak6.gif|left|200px]]
 
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==DESTRIN, NMR, MINIMIZED AVERAGE STRUCTURE==
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The line below this paragraph, containing "STRUCTURE_1ak6", creates the "Structure Box" on the page.
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<StructureSection load='1ak6' size='340' side='right'caption='[[1ak6]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1ak6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AK6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AK6 FirstGlance]. <br>
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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'>[https://proteopedia.org/fgij/fg.htm?mol=1ak6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ak6 OCA], [https://pdbe.org/1ak6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ak6 RCSB], [https://www.ebi.ac.uk/pdbsum/1ak6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ak6 ProSAT]</span></td></tr>
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{{STRUCTURE_1ak6| PDB=1ak6 | SCENE= }}
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</table>
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== Function ==
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'''DESTRIN, NMR, MINIMIZED AVERAGE STRUCTURE'''
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[https://www.uniprot.org/uniprot/DEST_PIG DEST_PIG] Actin-depolymerizing protein. Severs actin filaments (F-actin) and binds to actin monomers (G-actin). Acts in a pH-independent manner.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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==Overview==
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ak/1ak6_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ak6 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
Destrin is an isoprotein of cofilin that regulates actin cytoskeleton in various eukaryotes. We determined the tertiary structure of destrin by triple-resonance multidimensional nuclear magnetic resonance. In spite of there being no significant amino acid sequence homology, we found that the folding of destrin was strikingly similar to that of repeated segments in the gelsolin family, which resulted in a new protein fold group. Sequential dissimilarity of the actin-binding helix of destrin to that of gelsolin explains the Ca2+-independent actin-binding of destrin. Possible mechanisms of phosphorylation-sensitive phosphoinositide-competitive actin binding, of pH-dependent filament severing, and of nuclear translocation with actin in response to stresses, are discussed on the basis of the tertiary structure.
Destrin is an isoprotein of cofilin that regulates actin cytoskeleton in various eukaryotes. We determined the tertiary structure of destrin by triple-resonance multidimensional nuclear magnetic resonance. In spite of there being no significant amino acid sequence homology, we found that the folding of destrin was strikingly similar to that of repeated segments in the gelsolin family, which resulted in a new protein fold group. Sequential dissimilarity of the actin-binding helix of destrin to that of gelsolin explains the Ca2+-independent actin-binding of destrin. Possible mechanisms of phosphorylation-sensitive phosphoinositide-competitive actin binding, of pH-dependent filament severing, and of nuclear translocation with actin in response to stresses, are discussed on the basis of the tertiary structure.
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==About this Structure==
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Tertiary structure of destrin and structural similarity between two actin-regulating protein families.,Hatanaka H, Ogura K, Moriyama K, Ichikawa S, Yahara I, Inagaki F Cell. 1996 Jun 28;85(7):1047-55. PMID:8674111<ref>PMID:8674111</ref>
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1AK6 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens_and_sus_scrofa Homo sapiens and sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AK6 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Tertiary structure of destrin and structural similarity between two actin-regulating protein families., Hatanaka H, Ogura K, Moriyama K, Ichikawa S, Yahara I, Inagaki F, Cell. 1996 Jun 28;85(7):1047-55. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8674111 8674111]
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</div>
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[[Category: Homo sapiens and sus scrofa]]
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<div class="pdbe-citations 1ak6" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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== References ==
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[[Category: Hatanaka, H.]]
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<references/>
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[[Category: Ichikawa, S.]]
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__TOC__
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[[Category: Inagaki, F.]]
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</StructureSection>
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[[Category: Moriyama, K.]]
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[[Category: Homo sapiens]]
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[[Category: Ogura, K.]]
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[[Category: Large Structures]]
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[[Category: Yahara, I.]]
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[[Category: Sus scrofa]]
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[[Category: Actin depolymerization factor]]
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[[Category: Hatanaka H]]
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[[Category: Actin-binding protein]]
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[[Category: Ichikawa S]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:22:32 2008''
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[[Category: Inagaki F]]
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[[Category: Moriyama K]]
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[[Category: Ogura K]]
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[[Category: Yahara I]]

Current revision

DESTRIN, NMR, MINIMIZED AVERAGE STRUCTURE

PDB ID 1ak6

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