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1h6g

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(New page: 200px<br /> <applet load="1h6g" size="450" color="white" frame="true" align="right" spinBox="true" caption="1h6g, resolution 2.20&Aring;" /> '''ALPHA-CATENIN M-DOM...)
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Revision as of 15:06, 12 November 2007

Image:1h6g.gif

1h6g, resolution 2.20Å

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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

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