1H6G

alpha-catenin M-domain

Summary for 1H6G

• Entry DOI: 10.2210/pdb1h6g/pdb
• Descriptor: ALPHA-1 CATENIN, (4S)-2-METHYL-2,4-PENTANEDIOL, CALCIUM ION, ... (5 entities in total)
• Functional Keywords: alpha-catenin, adhesion modulation, cytoskeleton, cell adhesion
• Biological source: HOMO SAPIENS (HUMAN)
• Cellular location: Isoform 1: Cytoplasm, cytoskeleton. Isoform 3: Cell membrane ; Peripheral membrane protein ; Cytoplasmic side : P35221
• Total number of polymer chains: 2
• Total formula weight: 57995.22

Authors

Yang, J.,Dokurno, P.,Tonks, N.K.,Barford, D. (deposition date: 2001-06-14, release date: 2001-08-07, Last modification date: 2024-11-20)

Primary citation

Yang, J.,Dokurno, P.,Tonks, N.K.,Barford, D.
Crystal Structure of the M-Fragment of Alpha-Catenin: Implications for Modulation of Cell Adhesion.
Embo J., 20:3645-, 2001

PubMed Abstract: 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.

PubMed: 11447106
DOI: 10.1093/EMBOJ/20.14.3645

Experimental method

X-RAY DIFFRACTION (2.2 Å)