4igg: Difference between revisions
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==Full-length human alpha-catenin crystal structure== | ==Full-length human alpha-catenin crystal structure== | ||
<StructureSection load='4igg' size='340' side='right' caption='[[4igg]], [[Resolution|resolution]] 3.66Å' scene=''> | <StructureSection load='4igg' size='340' side='right'caption='[[4igg]], [[Resolution|resolution]] 3.66Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4igg]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4igg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IGG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4IGG FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=4igg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4igg OCA], [https://pdbe.org/4igg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4igg RCSB], [https://www.ebi.ac.uk/pdbsum/4igg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4igg ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/CTNA1_HUMAN CTNA1_HUMAN] 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. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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==See Also== | ==See Also== | ||
*[[Catenin|Catenin]] | *[[Catenin 3D structures|Catenin 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Izard T]] | ||
[[Category: | [[Category: Rangarajan ES]] | ||
Revision as of 23:43, 16 November 2022
Full-length human alpha-catenin crystal structureFull-length human alpha-catenin crystal structure
Structural highlights
FunctionCTNA1_HUMAN 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. Publication Abstract from PubMedThe F-actin-binding cytoskeletal protein alpha-catenin interacts with beta-catenin-cadherin complexes and stabilizes cell-cell junctions. The beta-catenin-alpha-catenin complex cannot bind F-actin, whereas interactions of alpha-catenin with the cytoskeletal protein vinculin appear to be necessary to stabilize adherens junctions. Here we report the crystal structure of nearly full-length human alpha-catenin at 3.7-A resolution. alpha-catenin forms an asymmetric dimer where the four-helix bundle domains of each subunit engage in distinct intermolecular interactions. This results in a left handshake-like dimer, wherein the two subunits have remarkably different conformations. The crystal structure explains why dimeric alpha-catenin has a higher affinity for F-actin than does monomeric alpha-catenin, why the beta-catenin-alpha-catenin complex does not bind F-actin, how activated vinculin links the cadherin-catenin complex to the cytoskeleton and why alpha-catenin but not inactive vinculin can bind F-actin. Dimer asymmetry defines alpha-catenin interactions.,Rangarajan ES, Izard T Nat Struct Mol Biol. 2013 Feb;20(2):188-93. doi: 10.1038/nsmb.2479. Epub 2013 Jan, 6. PMID:23292143[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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