1l7c
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| , resolution 2.50Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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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