This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
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...) |
|||
| Line 1: | Line 1: | ||
| - | [[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== | ||
| Line 15: | Line 14: | ||
[[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
|
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
Page seeded by OCA on Thu Feb 21 13:42:12 2008
