1h6g
From Proteopedia
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|PDB= 1h6g |SIZE=350|CAPTION= <scene name='initialview01'>1h6g</scene>, resolution 2.20Å | |PDB= 1h6g |SIZE=350|CAPTION= <scene name='initialview01'>1h6g</scene>, resolution 2.20Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |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> | ||
}} | }} | ||
| Line 26: | Line 29: | ||
[[Category: Tonks, N K.]] | [[Category: Tonks, N K.]] | ||
[[Category: Yang, J.]] | [[Category: Yang, J.]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: CL]] | ||
| - | [[Category: MPD]] | ||
[[Category: adhesion modulation]] | [[Category: adhesion modulation]] | ||
[[Category: alpha-catenin]] | [[Category: alpha-catenin]] | ||
[[Category: cytoskeleton]] | [[Category: cytoskeleton]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:58:43 2008'' |
Revision as of 17:58, 30 March 2008
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| , resolution 2.20Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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