1l7c
From Proteopedia
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- | [[Image:1l7c.gif|left|200px]] | + | [[Image:1l7c.gif|left|200px]] |
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- | '''alpha-catenin fragment, residues 385-651''' | + | {{Structure |
+ | |PDB= 1l7c |SIZE=350|CAPTION= <scene name='initialview01'>1l7c</scene>, resolution 2.50Å | ||
+ | |SITE= | ||
+ | |LIGAND= | ||
+ | |ACTIVITY= | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''alpha-catenin fragment, residues 385-651''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1L7C is a [ | + | 1L7C is a [[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== | ||
- | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11907041 11907041] |
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: four-helix bundle]] | [[Category: four-helix bundle]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:27:22 2008'' |
Revision as of 10:27, 20 March 2008
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, resolution 2.50Å | |||||||
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Coordinates: | save as pdb, mmCIF, xml |
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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