4igg: Difference between revisions
New page: {{STRUCTURE_4igg| PDB=4igg | SCENE= }} ===Full-length human alpha-catenin crystal structure=== {{ABSTRACT_PUBMED_23292143}} ==Function== [[http://www.uniprot.org/uniprot/CTNA1_HUMAN ... |
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Revision as of 07:19, 12 September 2013
Full-length human alpha-catenin crystal structureFull-length human alpha-catenin crystal structure
Template:ABSTRACT PUBMED 23292143
FunctionFunction
[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.
About this StructureAbout this Structure
4igg is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
- ↑ Rangarajan ES, Izard T. Dimer asymmetry defines alpha-catenin interactions. Nat Struct Mol Biol. 2013 Feb;20(2):188-93. doi: 10.1038/nsmb.2479. Epub 2013 Jan, 6. PMID:23292143 doi:10.1038/nsmb.2479