6dv1: Difference between revisions
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New page: '''Unreleased structure''' The entry 6dv1 is ON HOLD Authors: Ishiyama, N., Ikura, M. Description: Crystal structure of the alpha-E-catenin actin-binding domain [[Category: Unreleased ... |
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The | ==Crystal structure of the alpha-E-catenin actin-binding domain== | ||
<StructureSection load='6dv1' size='340' side='right'caption='[[6dv1]], [[Resolution|resolution]] 2.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6dv1]] 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=6DV1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6DV1 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=6dv1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dv1 OCA], [https://pdbe.org/6dv1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6dv1 RCSB], [https://www.ebi.ac.uk/pdbsum/6dv1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6dv1 ProSAT]</span></td></tr> | |||
</table> | |||
== 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> | |||
==See Also== | |||
*[[Catenin 3D structures|Catenin 3D structures]] | |||
== References == | |||
[[Category: | <references/> | ||
[[Category: Ikura | __TOC__ | ||
[[Category: Ishiyama | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Mus musculus]] | |||
[[Category: Ikura M]] | |||
[[Category: Ishiyama N]] | |||
Latest revision as of 17:36, 13 March 2024
Crystal structure of the alpha-E-catenin actin-binding domainCrystal structure of the alpha-E-catenin actin-binding domain
Structural highlights
FunctionCTNA1_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.[1] See AlsoReferences
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