1dk8

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spinqualitylabelsall models 1dk8, resolution 1.57Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CRYSTAL STRUCTURE OF THE RGS-HOMOLOGOUS DOMAIN OF AXIN

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

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: Caudal duplication anomaly OMIM:[603816], Hepatocellular carcinoma, somatic OMIM:[603816]

About this Structure

1DK8 is a Single protein structure of sequence from Homo sapiens with SO4, DTT and GOL as ligands. 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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