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1h6g

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1h6g, resolution 2.20Å ()
Ligands: , ,
Non-Standard Residues:
Domains: Vinculin
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



ALPHA-CATENIN M-DOMAIN

Publication Abstract from PubMed

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.

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

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

1H6G is a 2 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

  • Yang J, Dokurno P, Tonks NK, Barford D. Crystal structure of the M-fragment of alpha-catenin: implications for modulation of cell adhesion. EMBO J. 2001 Jul 16;20(14):3645-56. PMID:11447106

Page seeded by OCA on Tue Feb 17 14:47:48 2009

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