1jpp: Difference between revisions

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[[Image:1jpp.~~gif~~|left|200px]]

[[Image:1jpp.png|left|200px]]

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~~'''~~The Structure of a beta-Catenin Binding Repeat from Adenomatous Polyposis Coli (APC) in Complex with beta-Catenin~~'''~~

===The Structure of a beta-Catenin Binding Repeat from Adenomatous Polyposis Coli (APC) in Complex with beta-Catenin===

~~==Overview==~~

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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.

The line below this paragraph, {{ABSTRACT_PUBMED_11707392}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 11707392 is the PubMed ID number.

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==About this Structure==

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[[Category: Disease mutation]]

[[Category: Repeat]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ ~~2 21~~:34:02 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 20:36:25 2008''

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-[[Image:1jpp.gif|left|200px]]
+{{Seed}}
+[[Image:1jpp.png|left|200px]]
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 {{STRUCTURE_1jpp|  PDB=1jpp  |  SCENE=  }}
-'''The Structure of a beta-Catenin Binding Repeat from Adenomatous Polyposis Coli (APC) in Complex with beta-Catenin'''
+===The Structure of a beta-Catenin Binding Repeat from Adenomatous Polyposis Coli (APC) in Complex with beta-Catenin===
-==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.
+The line below this paragraph, {{ABSTRACT_PUBMED_11707392}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11707392 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11707392}}
 ==About this Structure==
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 [[Category: Disease mutation]]
 [[Category: Repeat]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 21:34:02 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 20:36:25 2008''