1h6g
From Proteopedia
(New page: 200px<br /> <applet load="1h6g" size="450" color="white" frame="true" align="right" spinBox="true" caption="1h6g, resolution 2.20Å" /> '''ALPHA-CATENIN M-DOM...) |
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| - | [[Image:1h6g.gif|left|200px]]<br /> | + | [[Image:1h6g.gif|left|200px]]<br /><applet load="1h6g" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1h6g" size=" | + | |
caption="1h6g, resolution 2.20Å" /> | caption="1h6g, resolution 2.20Å" /> | ||
'''ALPHA-CATENIN M-DOMAIN'''<br /> | '''ALPHA-CATENIN M-DOMAIN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The cytoskeletal protein alpha-catenin, which shares structural similarity | + | 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== | ==About this Structure== | ||
| - | 1H6G is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CA, CL and MPD as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1H6G is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=MPD:'>MPD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H6G OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Barford, D.]] | [[Category: Barford, D.]] | ||
[[Category: Dokurno, P.]] | [[Category: Dokurno, P.]] | ||
| - | [[Category: Tonks, N | + | [[Category: Tonks, N K.]] |
[[Category: Yang, J.]] | [[Category: Yang, J.]] | ||
[[Category: CA]] | [[Category: CA]] | ||
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[[Category: cytoskeleton]] | [[Category: cytoskeleton]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:57:55 2008'' |
Revision as of 10:58, 21 February 2008
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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 , and 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
Page seeded by OCA on Thu Feb 21 12:57:55 2008
Categories: Homo sapiens | Single protein | Barford, D. | Dokurno, P. | Tonks, N K. | Yang, J. | CA | CL | MPD | Adhesion modulation | Alpha-catenin | Cytoskeleton
