1DK8: Crystal Structure of the Rgs-homologous Domain of Axin

Citation:
Abstract
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.
PDB ID: 1DK8Download
MMDB ID: 13911
PDB Deposition Date: 1999/12/6
Updated in MMDB: 2012/10 
Experimental Method:
x-ray diffraction
Resolution: 1.57  Å
Source Organism:
Similar Structures:
Biological Unit for 1DK8: dimeric; determined by author
Molecular Components in 1DK8
Label Count Molecule
Proteins (2 molecules)
2
Axin
Molecule annotation
Chemicals (20 molecules)
1
12
2
2
3
6
* Click molecule labels to explore molecular sequence information.

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