1l7c
From Proteopedia
(New page: 200px<br /> <applet load="1l7c" size="450" color="white" frame="true" align="right" spinBox="true" caption="1l7c, resolution 2.50Å" /> '''alpha-catenin fragm...) |
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| - | [[Image:1l7c.gif|left|200px]]<br /> | + | [[Image:1l7c.gif|left|200px]]<br /><applet load="1l7c" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1l7c" size=" | + | |
caption="1l7c, resolution 2.50Å" /> | caption="1l7c, resolution 2.50Å" /> | ||
'''alpha-catenin fragment, residues 385-651'''<br /> | '''alpha-catenin fragment, residues 385-651'''<br /> | ||
==Overview== | ==Overview== | ||
| - | alpha-Catenin is an integral component of adherens junctions, where it | + | alpha-Catenin is an integral component of adherens junctions, where it links cadherins to the actin cytoskeleton. alpha-Catenin is also required for the colocalization of the nectin/afadin/ponsin adhesion system to adherens junctions, and it specifically associates with the nectin-binding protein afadin. A proteolytic fragment of alpha-catenin, residues 385-651, contains the afadin-binding site. The three-dimensional structure of this fragment comprises two side-by-side four-helix bundles, both of which are required for afadin binding. The alpha-catenin fragment 385-651 binds afadin more strongly than the full-length protein, suggesting that the full-length protein harbors a cryptic binding site for afadin. Comparison of the alpha-catenin 385-651 structure with the recently solved structure of the alpha-catenin M-fragment (Yang, J., Dokurno, P., Tonks, N. K., and Barford, D. (2001) EMBO J. 20, 3645-3656) reveals a surprising flexibility in the orientation of the two four-helix bundles. alpha-Catenin and the actin-binding protein vinculin share sequence and most likely structural similarity within their actin-binding domains. Despite this homology, actin binding requires additional sequences adjacent to this region. |
==About this Structure== | ==About this Structure== | ||
| - | 1L7C is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http:// | + | 1L7C is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L7C OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Drees, F.]] | [[Category: Drees, F.]] | ||
| - | [[Category: Nelson, W | + | [[Category: Nelson, W J.]] |
[[Category: Pokutta, S.]] | [[Category: Pokutta, S.]] | ||
[[Category: Takai, Y.]] | [[Category: Takai, Y.]] | ||
| - | [[Category: Weis, W | + | [[Category: Weis, W I.]] |
[[Category: four-helix bundle]] | [[Category: four-helix bundle]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:42:12 2008'' |
Revision as of 11:42, 21 February 2008
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alpha-catenin fragment, residues 385-651
Overview
alpha-Catenin is an integral component of adherens junctions, where it links cadherins to the actin cytoskeleton. alpha-Catenin is also required for the colocalization of the nectin/afadin/ponsin adhesion system to adherens junctions, and it specifically associates with the nectin-binding protein afadin. A proteolytic fragment of alpha-catenin, residues 385-651, contains the afadin-binding site. The three-dimensional structure of this fragment comprises two side-by-side four-helix bundles, both of which are required for afadin binding. The alpha-catenin fragment 385-651 binds afadin more strongly than the full-length protein, suggesting that the full-length protein harbors a cryptic binding site for afadin. Comparison of the alpha-catenin 385-651 structure with the recently solved structure of the alpha-catenin M-fragment (Yang, J., Dokurno, P., Tonks, N. K., and Barford, D. (2001) EMBO J. 20, 3645-3656) reveals a surprising flexibility in the orientation of the two four-helix bundles. alpha-Catenin and the actin-binding protein vinculin share sequence and most likely structural similarity within their actin-binding domains. Despite this homology, actin binding requires additional sequences adjacent to this region.
About this Structure
1L7C is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Biochemical and structural definition of the l-afadin- and actin-binding sites of alpha-catenin., Pokutta S, Drees F, Takai Y, Nelson WJ, Weis WI, J Biol Chem. 2002 May 24;277(21):18868-74. Epub 2002 Mar 20. PMID:11907041
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