1emu
From Proteopedia
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| - | [[Image:1emu.jpg|left|200px]] | + | [[Image:1emu.jpg|left|200px]] |
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| - | '''STRUCTURE OF THE AXIN RGS-HOMOLOGOUS DOMAIN IN COMPLEX WITH A SAMP REPEAT FROM APC''' | + | {{Structure |
| + | |PDB= 1emu |SIZE=350|CAPTION= <scene name='initialview01'>1emu</scene>, resolution 1.90Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''STRUCTURE OF THE AXIN RGS-HOMOLOGOUS DOMAIN IN COMPLEX WITH A SAMP REPEAT FROM APC''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1EMU is a [ | + | 1EMU is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EMU OCA]. |
==Reference== | ==Reference== | ||
| - | Structural basis of the Axin-adenomatous polyposis coli interaction., Spink KE, Polakis P, Weis WI, EMBO J. 2000 May 15;19(10):2270-9. PMID:[http:// | + | Structural basis of the Axin-adenomatous polyposis coli interaction., Spink KE, Polakis P, Weis WI, EMBO J. 2000 May 15;19(10):2270-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10811618 10811618] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: rgs domain]] | [[Category: rgs domain]] | ||
| - | ''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 10:57:47 2008'' |
Revision as of 08:57, 20 March 2008
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| , resolution 1.90Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF THE AXIN RGS-HOMOLOGOUS DOMAIN IN COMPLEX WITH A SAMP REPEAT FROM APC
Contents |
Overview
Axin and the adenomatous polyposis coli (APC) tumor suppressor protein are components of the Wnt/Wingless growth factor signaling pathway. In the absence of Wnt signal, Axin and APC regulate cytoplasmic levels of the proto-oncogene beta-catenin through the formation of a large complex containing these three proteins, glycogen synthase kinase 3beta (GSK3beta) and several other proteins. Both Axin and APC are known to be critical for beta-catenin regulation, and truncations in APC that eliminate the Axin-binding site result in human cancers. A protease-resistant domain of Axin that contains the APC-binding site is a member of the regulators of G-protein signaling (RGS) superfamily. The crystal structures of this domain alone and in complex with an Axin-binding sequence from APC reveal that the Axin-APC interaction occurs at a conserved groove on a face of the protein that is distinct from the G-protein interface of classical RGS proteins. The molecular interactions observed in the Axin-APC complex provide a rationale for the evolutionary conservation seen in both proteins.
Disease
Known diseases associated with this structure: Adenoma, periampullary OMIM:[611731], Adenomatous polyposis coli OMIM:[611731], Brain tumor-polyposis syndrome 2 OMIM:[611731], Caudal duplication anomaly OMIM:[603816], Colorectal cancer, somatic OMIM:[611731], Desmoid disease, hereditary OMIM:[611731], Gardner syndrome OMIM:[611731], Gastric cancer, somatic OMIM:[611731], Hepatoblastoma OMIM:[611731], Hepatocellular carcinoma, somatic OMIM:[603816]
About this Structure
1EMU is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural basis of the Axin-adenomatous polyposis coli interaction., Spink KE, Polakis P, Weis WI, EMBO J. 2000 May 15;19(10):2270-9. PMID:10811618
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