4k1n

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{{STRUCTURE_4k1n| PDB=4k1n | SCENE= }}
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==Crystal structure of full-length mouse alphaE-catenin==
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===Crystal structure of full-length mouse alphaE-catenin===
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<StructureSection load='4k1n' size='340' side='right' caption='[[4k1n]], [[Resolution|resolution]] 6.50&Aring;' scene=''>
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{{ABSTRACT_PUBMED_23589308}}
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4k1n]] is a 2 chain structure 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=4K1N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4K1N FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4k1o|4k1o]]</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Catna1, Ctnna1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])</td></tr>
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<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=4k1n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k1n OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4k1n RCSB], [http://www.ebi.ac.uk/pdbsum/4k1n PDBsum]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==Function==
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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>
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[[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>
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[4k1n]] is a 2 chain structure 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=4K1N OCA].
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</div>
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==Reference==
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==See Also==
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<ref group="xtra">PMID:023589308</ref><references group="xtra"/><references/>
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*[[Catenin|Catenin]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Ikura, M.]]
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[[Category: Ikura, M]]
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[[Category: Ishiyama, N.]]
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[[Category: Ishiyama, N]]
[[Category: Beta-catenin]]
[[Category: Beta-catenin]]
[[Category: Cell adhesion]]
[[Category: Cell adhesion]]
[[Category: F-actin]]
[[Category: F-actin]]
[[Category: Four-helix bundle]]
[[Category: Four-helix bundle]]

Revision as of 14:43, 21 December 2014

Crystal structure of full-length mouse alphaE-catenin

4k1n, resolution 6.50Å

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