1jpp
From Proteopedia
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| - | [[Image:1jpp.gif|left|200px]] | + | [[Image:1jpp.gif|left|200px]] |
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| - | '''The Structure of a beta-Catenin Binding Repeat from Adenomatous Polyposis Coli (APC) in Complex with beta-Catenin''' | + | {{Structure |
| + | |PDB= 1jpp |SIZE=350|CAPTION= <scene name='initialview01'>1jpp</scene>, resolution 3.10Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''The Structure of a beta-Catenin Binding Repeat from Adenomatous Polyposis Coli (APC) in Complex with beta-Catenin''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1JPP is a [ | + | 1JPP is a [[Protein complex]] structure of sequences 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=1JPP OCA]. |
==Reference== | ==Reference== | ||
| - | Molecular mechanisms of beta-catenin recognition by adenomatous polyposis coli revealed by the structure of an APC-beta-catenin complex., Eklof Spink K, Fridman SG, Weis WI, EMBO J. 2001 Nov 15;20(22):6203-12. PMID:[http:// | + | Molecular mechanisms of beta-catenin recognition by adenomatous polyposis coli revealed by the structure of an APC-beta-catenin complex., Eklof Spink K, Fridman SG, Weis WI, EMBO J. 2001 Nov 15;20(22):6203-12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11707392 11707392] |
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: repeat]] | [[Category: repeat]] | ||
| - | ''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 12:06:41 2008'' |
Revision as of 10:06, 20 March 2008
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| , resolution 3.10Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
The Structure of a beta-Catenin Binding Repeat from Adenomatous Polyposis Coli (APC) in Complex with beta-Catenin
Contents |
Overview
The adenomatous polyposis coli (APC) tumor suppressor protein plays a critical role in regulating cellular levels of the oncogene product beta-catenin. APC binds to beta-catenin through a series of homologous 15 and 20 amino acid repeats. We have determined the crystal structure of a 15 amino acid beta-catenin binding repeat from APC bound to the armadillo repeat region of beta-catenin. Although it lacks significant sequence homology, the N-terminal half of the repeat binds in a manner similar to portions of E-cadherin and XTcf3, but the remaining interactions are unique to APC. We discuss the implications of this new structure for the design of therapeutics, and present evidence from structural, biochemical and sequence data, which suggest that the 20 amino acid repeats can adopt two modes of binding to beta-catenin.
Disease
Known diseases associated with this structure: Adenoma, periampullary OMIM:[611731], Adenomatous polyposis coli OMIM:[611731], Brain tumor-polyposis syndrome 2 OMIM:[611731], Colorectal cancer, somatic OMIM:[611731], Desmoid disease, hereditary OMIM:[611731], Gardner syndrome OMIM:[611731], Gastric cancer, somatic OMIM:[611731], Hepatoblastoma OMIM:[611731]
About this Structure
1JPP is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
Reference
Molecular mechanisms of beta-catenin recognition by adenomatous polyposis coli revealed by the structure of an APC-beta-catenin complex., Eklof Spink K, Fridman SG, Weis WI, EMBO J. 2001 Nov 15;20(22):6203-12. PMID:11707392
Page seeded by OCA on Thu Mar 20 12:06:41 2008
