1L7C

alpha-catenin fragment, residues 385-651

Summary for 1L7C

• Entry DOI: 10.2210/pdb1l7c/pdb
• Descriptor: Alpha E-catenin (2 entities in total)
• Functional Keywords: four-helix bundle, cell adhesion
• Biological source: Mus musculus (house mouse)
• Cellular location: Cytoplasm, cytoskeleton: P35221
• Total number of polymer chains: 3
• Total formula weight: 90620.90

Authors

Pokutta, S.,Drees, F.,Takai, Y.,Nelson, W.J.,Weis, W.I. (deposition date: 2002-03-14, release date: 2002-06-19, Last modification date: 2024-11-06)

Primary citation

Pokutta, S.,Drees, F.,Takai, Y.,Nelson, W.J.,Weis, W.I.
Biochemical and structural definition of the l-afadin- and actin-binding sites of alpha-catenin.
J.Biol.Chem., 277:18868-18874, 2002

PubMed Abstract: 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.

PubMed: 11907041
DOI: 10.1074/jbc.M201463200

Experimental method

X-RAY DIFFRACTION (2.5 Å)