1l7c
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alpha-catenin fragment, residues 385-651
OverviewOverview
alpha-Catenin is an integral component of adherens junctions, where it, links cadherins to the actin cytoskeleton. alpha-Catenin is also required, for the colocalization of the nectin/afadin/ponsin adhesion system to, adherens junctions, and it specifically associates with the nectin-binding, protein afadin. A proteolytic fragment of alpha-catenin, residues 385-651, contains the afadin-binding site. The three-dimensional structure of this, fragment comprises two side-by-side four-helix bundles, both of which are, required for afadin binding. The alpha-catenin fragment 385-651 binds, afadin more strongly than the full-length protein, suggesting that the, full-length protein harbors a cryptic binding site for afadin. Comparison, of the alpha-catenin 385-651 structure with the recently solved structure, of the alpha-catenin M-fragment (Yang, J., Dokurno, P., Tonks, N. K., and, Barford, D. (2001) EMBO J. 20, 3645-3656) reveals a surprising flexibility, in the orientation of the two four-helix bundles. alpha-Catenin and the, actin-binding protein vinculin share sequence and most likely structural, similarity within their actin-binding domains. Despite this homology, actin binding requires additional sequences adjacent to this region.
About this StructureAbout this Structure
1L7C is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
ReferenceReference
Biochemical and structural definition of the l-afadin- and actin-binding sites of alpha-catenin., Pokutta S, Drees F, Takai Y, Nelson WJ, Weis WI, J Biol Chem. 2002 May 24;277(21):18868-74. Epub 2002 Mar 20. PMID:11907041
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