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[[Image:1udm.gif|left|200px]]


{{Structure
==Solution structure of Coactosin-like protein (Cofilin family) from Mus Musculus==
|PDB= 1udm |SIZE=350|CAPTION= <scene name='initialview01'>1udm</scene>
<StructureSection load='1udm' size='340' side='right'caption='[[1udm]]' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND=  
<table><tr><td colspan='2'>[[1udm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UDM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UDM FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
|GENE= RIKEN cDNA 2010004C08 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1udm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1udm OCA], [https://pdbe.org/1udm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1udm RCSB], [https://www.ebi.ac.uk/pdbsum/1udm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1udm ProSAT], [https://www.topsan.org/Proteins/RSGI/1udm TOPSAN]</span></td></tr>
|DOMAIN=
</table>
|RELATEDENTRY=
== Function ==
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1udm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1udm OCA], [http://www.ebi.ac.uk/pdbsum/1udm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1udm RCSB]</span>
[https://www.uniprot.org/uniprot/COTL1_MOUSE COTL1_MOUSE] Binds to F-actin in a calcium-independent manner. Has no direct effect on actin depolymerization.<ref>PMID:11785969</ref>
}}
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ud/1udm_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1udm ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Actin is one of the most conserved proteins in nature. Its assembly and disassembly are regulated by many proteins, including the family of actin-depolymerizing factor homology (ADF-H) domains. ADF-H domains can be divided into five classes: ADF/cofilin, glia maturation factor (GMF), coactosin, twinfilin, and Abp1/drebrin. The best-characterized class is ADF/cofilin. The other four classes have drawn much less attention and very few structures have been reported. This study presents the solution NMR structure of the ADF-H domain of human HIP-55-drebrin-like protein, the first published structure of a drebrin-like domain (mammalian), and the first published structure of GMF beta (mouse). We also determined the structures of mouse GMF gamma, the mouse coactosin-like domain and the C-terminal ADF-H domain of mouse twinfilin 1. Although the overall fold of the five domains is similar, some significant differences provide valuable insights into filamentous actin (F-actin) and globular actin (G-actin) binding, including the identification of binding residues on the long central helix. This long helix is stabilized by three or four residues. Notably, the F-actin binding sites of mouse GMF beta and GMF gamma contain two additional beta-strands not seen in other ADF-H structures. The G-actin binding site of the ADF-H domain of human HIP-55-drebrin-like protein is absent and distorted in mouse GMF beta and GMF gamma.


'''Solution structure of Coactosin-like protein (Cofilin family) from Mus Musculus'''
NMR solution structures of actin depolymerizing factor homology domains.,Goroncy AK, Koshiba S, Tochio N, Tomizawa T, Sato M, Inoue M, Watanabe S, Hayashizaki Y, Tanaka A, Kigawa T, Yokoyama S Protein Sci. 2009 Nov;18(11):2384-92. PMID:19768801<ref>PMID:19768801</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
==About this Structure==
</div>
1UDM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UDM OCA].
<div class="pdbe-citations 1udm" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Goroncy AK]]
[[Category: Goroncy, A.]]
[[Category: Inoue M]]
[[Category: Inoue, M.]]
[[Category: Kigawa T]]
[[Category: Kigawa, T.]]
[[Category: Kobayashi N]]
[[Category: Kobayashi, N.]]
[[Category: Koshiba S]]
[[Category: Koshiba, S.]]
[[Category: Tochio N]]
[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
[[Category: Yokoyama S]]
[[Category: Tochio, N.]]
[[Category: Yokoyama, S.]]
[[Category: actin binding protein]]
[[Category: cytoskeletal]]
[[Category: riken structural genomics/proteomics initiative]]
[[Category: rsgi]]
[[Category: structural genomic]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:08:49 2008''

Latest revision as of 23:51, 27 December 2023

Solution structure of Coactosin-like protein (Cofilin family) from Mus Musculus

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