4k1o: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4k1o]] 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=4K1O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4K1O FirstGlance]. <br>
<table><tr><td colspan='2'>[[4k1o]] 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=4K1O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4K1O FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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]] 2.603&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=4k1o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k1o OCA], [https://pdbe.org/4k1o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4k1o RCSB], [https://www.ebi.ac.uk/pdbsum/4k1o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4k1o ProSAT]</span></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=4k1o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k1o OCA], [https://pdbe.org/4k1o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4k1o RCSB], [https://www.ebi.ac.uk/pdbsum/4k1o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4k1o ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/CTNA2_MOUSE CTNA2_MOUSE] May function as a linker between cadherin adhesion receptors and the cytoskeleton to regulate cell-cell adhesion and differentiation in the nervous system. Regulates morphological plasticity of synapses and cerebellar and hippocampal lamination during development. Functions in the control of startle modulation.<ref>PMID:12089526</ref> <ref>PMID:12123610</ref> <ref>PMID:15034585</ref>  
[https://www.uniprot.org/uniprot/CTNA2_MOUSE CTNA2_MOUSE] May function as a linker between cadherin adhesion receptors and the cytoskeleton to regulate cell-cell adhesion and differentiation in the nervous system. Regulates morphological plasticity of synapses and cerebellar and hippocampal lamination during development. Functions in the control of startle modulation.<ref>PMID:12089526</ref> <ref>PMID:12123610</ref> <ref>PMID:15034585</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
alpha-catenin is an actin- and vinculin-binding protein that regulates cell-cell adhesion by interacting with cadherin adhesion receptors through beta-catenin, but the mechanisms by which it anchors the cadherin-catenin complex to the actin cytoskeleton at adherens junctions remain unclear. Here we determined crystal structures of alphaE-catenin in the autoinhibited state and the actin-binding domain of alphaN-catenin. Together with the small-angle X-ray scattering analysis of full-length alphaN-catenin, we deduced an elongated multidomain assembly of monomeric alpha-catenin that structurally and functionally couples the vinculin- and actin-binding mechanisms. Cellular and biochemical studies of alphaE- and alphaN-catenins show that alphaE-catenin recruits vinculin to adherens junctions more effectively than alphaN-catenin, partly owing to its higher affinity for actin filaments. We propose a molecular switch mechanism involving multi-state conformational changes of alpha-catenin. This would be driven by actomyosin-generated tension to dynamically regulate the vinculin-assisted linkage between adherens junctions and the actin cytoskeleton.
An Autoinhibited Structure of alpha-catenin and Its Implications for Vinculin Recruitment to Adherens Junctions.,Ishiyama N, Tanaka N, Abe K, Yang YJ, Abbas YM, Umitsu M, Nagar B, Bueler SA, Rubinstein JL, Takeichi M, Ikura M J Biol Chem. 2013 Apr 15. PMID:23589308<ref>PMID:23589308</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4k1o" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
Retrieved from "https://proteopedia.org/4k1o"