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==DESTRIN, NMR, 20 STRUCTURES==
==DESTRIN, NMR, 20 STRUCTURES==
<StructureSection load='1ak7' size='340' side='right'caption='[[1ak7]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
<StructureSection load='1ak7' size='340' side='right'caption='[[1ak7]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1ak7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pig Pig]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AK7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AK7 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1ak7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AK7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AK7 FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ak6|1ak6]]</div></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ak7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ak7 OCA], [https://pdbe.org/1ak7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ak7 RCSB], [https://www.ebi.ac.uk/pdbsum/1ak7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ak7 ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ak7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ak7 OCA], [https://pdbe.org/1ak7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ak7 RCSB], [https://www.ebi.ac.uk/pdbsum/1ak7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ak7 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/DEST_HUMAN DEST_HUMAN]] Actin-depolymerizing protein. Severs actin filaments (F-actin) and binds to actin monomers (G-actin). Acts in a pH-independent manner.  
[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.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=1ak7 ConSurf].
</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=1ak7 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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.
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>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1ak7" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Pig]]
[[Category: Sus scrofa]]
[[Category: Hatanaka, H]]
[[Category: Hatanaka H]]
[[Category: Ichikawa, S]]
[[Category: Ichikawa S]]
[[Category: Inagaki, F]]
[[Category: Inagaki F]]
[[Category: Moriyama, K]]
[[Category: Moriyama K]]
[[Category: Ogura, K]]
[[Category: Ogura K]]
[[Category: Yahara, I]]
[[Category: Yahara I]]
[[Category: Actin depolymerization factor]]

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