1h6g

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[[Image:1h6g.gif|left|200px]]
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{{Structure
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The line below this paragraph, containing "STRUCTURE_1h6g", creates the "Structure Box" on the page.
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1h6g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h6g OCA], [http://www.ebi.ac.uk/pdbsum/1h6g PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1h6g RCSB]</span>
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'''ALPHA-CATENIN M-DOMAIN'''
'''ALPHA-CATENIN M-DOMAIN'''
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[[Category: Tonks, N K.]]
[[Category: Tonks, N K.]]
[[Category: Yang, J.]]
[[Category: Yang, J.]]
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[[Category: adhesion modulation]]
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[[Category: Adhesion modulation]]
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[[Category: alpha-catenin]]
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[[Category: Alpha-catenin]]
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[[Category: cytoskeleton]]
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[[Category: Cytoskeleton]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:29:40 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:58:43 2008''
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Revision as of 15:29, 2 May 2008

Image:1h6g.gif

Template:STRUCTURE 1h6g

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. 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 Fri May 2 18:29:40 2008

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