6o3e: Difference between revisions

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<StructureSection load='6o3e' size='340' side='right'caption='[[6o3e]], [[Resolution|resolution]] 4.00&Aring;' scene=''>
<StructureSection load='6o3e' size='340' side='right'caption='[[6o3e]], [[Resolution|resolution]] 4.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6o3e]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6O3E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6O3E FirstGlance]. <br>
<table><tr><td colspan='2'>[[6o3e]] is a 2 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=6O3E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6O3E FirstGlance]. <br>
</td></tr><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=6o3e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6o3e OCA], [http://pdbe.org/6o3e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6o3e RCSB], [http://www.ebi.ac.uk/pdbsum/6o3e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6o3e ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 4.001&#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=6o3e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6o3e OCA], [https://pdbe.org/6o3e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6o3e RCSB], [https://www.ebi.ac.uk/pdbsum/6o3e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6o3e ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://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>
[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>  
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 6o3e" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 6o3e" style="background-color:#fffaf0;"></div>
==See Also==
*[[Catenin 3D structures|Catenin 3D structures]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Pokutta, S]]
[[Category: Mus musculus]]
[[Category: Weis, W I]]
[[Category: Pokutta S]]
[[Category: Actin binding]]
[[Category: Weis WI]]
[[Category: Catenin]]
[[Category: Cell adhesion]]
Retrieved from "https://proteopedia.org/6o3e"