1dov: Difference between revisions

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[[Image:1dov.png|left|200px]]


{{STRUCTURE_1dov|  PDB=1dov  |  SCENE=  }}
==CRYSTAL STRUCTURE OF THE ALPHA-CATENIN DIMERIZATION DOMAIN==
 
<StructureSection load='1dov' size='340' side='right'caption='[[1dov]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
===CRYSTAL STRUCTURE OF THE ALPHA-CATENIN DIMERIZATION DOMAIN===
== Structural highlights ==
 
<table><tr><td colspan='2'>[[1dov]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DOV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DOV FirstGlance]. <br>
{{ABSTRACT_PUBMED_10882138}}
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</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=1dov FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dov OCA], [https://pdbe.org/1dov PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dov RCSB], [https://www.ebi.ac.uk/pdbsum/1dov PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dov ProSAT]</span></td></tr>
==About this Structure==
</table>
[[1dov]] is a 1 chain structure of [[Catenin]] with 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=1DOV OCA].  
== Function ==
[https://www.uniprot.org/uniprot/CTNA1_MOUSE CTNA1_MOUSE] Associates with the cytoplasmic domain of a variety of cadherins. The association of catenins to cadherins produces a complex which is linked to the actin filament network, and which seems to be of primary importance for cadherins cell-adhesion properties. Can associate with both E- and N-cadherins. Originally believed to be a stable component of E-cadherin/catenin adhesion complexes and to mediate the linkage of cadherins to the actin cytoskeleton at adherens junctions. In contrast, cortical actin was found to be much more dynamic than E-cadherin/catenin complexes and CTNNA1 was shown not to bind to F-actin when assembled in the complex suggesting a different linkage between actin and adherens junctions components. The homodimeric form may regulate actin filament assembly and inhibit actin branching by competing with the Arp2/3 complex for binding to actin filaments. May play a crucial role in cell differentiation.<ref>PMID:16325583</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/do/1dov_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=1dov ConSurf].
<div style="clear:both"></div>


==See Also==
==See Also==
*[[Catenin|Catenin]]
*[[Catenin 3D structures|Catenin 3D structures]]
 
*[[Phosphoribosyltransferase 3D structures|Phosphoribosyltransferase 3D structures]]
==Reference==
== References ==
<ref group="xtra">PMID:010882138</ref><ref group="xtra">PMID:015195105</ref><references group="xtra"/>
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Pokutta, S.]]
[[Category: Pokutta S]]
[[Category: Weis, W I.]]
[[Category: Weis WI]]
[[Category: Cell adhesion]]
[[Category: Four-helix bundle]]