1h6g
From Proteopedia
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ALPHA-CATENIN M-DOMAIN
Overview
The cytoskeletal protein alpha-catenin, which shares structural similarity, with vinculin, is required for cadherin-mediated cell adhesion, and, functions to modulate cell adhesive strength and to link the cadherins to, the actin-based cytoskeleton. Here we describe the crystal structure of a, region of alpha-catenin (residues 377-633) termed the M-fragment. The, M-fragment is composed of a tandem repeat of two antiparallel four-helix, bundles of virtually identical architectures that are related in structure, to the dimerization domain of alpha-catenin and the tail region of, vinculin. These results suggest that alpha-catenin is composed of, repeating antiparallel helical domains. The region of alpha-catenin, previously defined as an adhesion modulation domain corresponds to the, C-terminal four-helix bundle of the M-fragment, and in the crystal lattice, these domains exist as dimers. Evidence for dimerization of the M-fragment, of alpha-catenin in solution was detected by chemical cross-linking, experiments. The tendency of the adhesion modulation domain to form dimers, may explain its biological activity of promoting cell-cell adhesiveness by, inducing lateral dimerization of the associated cadherin molecule.
About this Structure
1H6G is a Single protein structure of sequence from Homo sapiens with CA, CL and MPD as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of the M-fragment of alpha-catenin: implications for modulation of cell adhesion., Yang J, Dokurno P, Tonks NK, Barford D, EMBO J. 2001 Jul 16;20(14):3645-56. PMID:11447106
Page seeded by OCA on Mon Nov 12 17:13:18 2007
Categories: Homo sapiens | Single protein | Barford, D. | Dokurno, P. | Tonks, N.K. | Yang, J. | CA | CL | MPD | Adhesion modulation | Alpha-catenin | Cytoskeleton
