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New page: left|200px<br /> <applet load="1jpp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jpp, resolution 3.10Å" /> '''The Structure of a ...
 
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[[Image:1jpp.gif|left|200px]]<br />
[[Image:1jpp.gif|left|200px]]<br /><applet load="1jpp" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1jpp" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1jpp, resolution 3.10&Aring;" />
caption="1jpp, resolution 3.10&Aring;" />
'''The Structure of a beta-Catenin Binding Repeat from Adenomatous Polyposis Coli (APC) in Complex with beta-Catenin'''<br />
'''The Structure of a beta-Catenin Binding Repeat from Adenomatous Polyposis Coli (APC) in Complex with beta-Catenin'''<br />


==Overview==
==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 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==
==Disease==
Known diseases associated with this structure: Adenoma, periampullary OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=175100 175100]], Adenomatous polyposis coli OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=175100 175100]], Adenomatous polyposis coli, attenuated OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=175100 175100]], Colorectal cancer OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=175100 175100]], Desmoid disease, hereditary OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=175100 175100]], Gardner syndrome OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=175100 175100]], Gastric cancer OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=175100 175100]], Turcot syndrome OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=175100 175100]]
Known diseases associated with this structure: Adenoma, periampullary OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=611731 611731]], Adenomatous polyposis coli OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=611731 611731]], Brain tumor-polyposis syndrome 2 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=611731 611731]], Colorectal cancer, somatic OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=611731 611731]], Desmoid disease, hereditary OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=611731 611731]], Gardner syndrome OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=611731 611731]], Gastric cancer, somatic OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=611731 611731]], Hepatoblastoma OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=611731 611731]]


==About this Structure==
==About this Structure==
1JPP is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with GOL as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JPP OCA].  
1JPP is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JPP OCA].  


==Reference==
==Reference==
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Fridman, S.G.]]
[[Category: Fridman, S G.]]
[[Category: Spink, K.E.]]
[[Category: Spink, K E.]]
[[Category: Weis, W.I.]]
[[Category: Weis, W I.]]
[[Category: GOL]]
[[Category: GOL]]
[[Category: anti-oncogene]]
[[Category: anti-oncogene]]
Line 25: Line 24:
[[Category: repeat]]
[[Category: repeat]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:25:19 2008''
Retrieved from "https://proteopedia.org/1jpp"