4k1n

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'''Unreleased structure'''
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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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{{ABSTRACT_PUBMED_23589308}}
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The entry 4k1n is ON HOLD
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==Function==
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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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Authors: Ishiyama, N., Ikura, M.
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==About this Structure==
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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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Description: Crystal structure of full-length mouse alphaE-catenin
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==Reference==
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<references group="xtra"/><references/>
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[[Category: Mus musculus]]
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[[Category: Ikura, M.]]
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[[Category: Ishiyama, N.]]
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[[Category: Beta-catenin]]
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[[Category: Cell adhesion]]
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[[Category: F-actin]]
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[[Category: Four-helix bundle]]

Revision as of 07:39, 2 May 2013

Template:STRUCTURE 4k1n

Contents

Crystal structure of full-length mouse alphaE-catenin

Template:ABSTRACT PUBMED 23589308

Function

[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.[1]

About this Structure

4k1n is a 2 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

  1. ↑ Drees F, Pokutta S, Yamada S, Nelson WJ, Weis WI. Alpha-catenin is a molecular switch that binds E-cadherin-beta-catenin and regulates actin-filament assembly. Cell. 2005 Dec 2;123(5):903-15. PMID:16325583 doi:10.1016/j.cell.2005.09.021

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