1DK8

CRYSTAL STRUCTURE OF THE RGS-HOMOLOGOUS DOMAIN OF AXIN

Summary for 1DK8

• Entry DOI: 10.2210/pdb1dk8/pdb
• Related: 1AGR 1CMZ 1EMU
• Descriptor: AXIN, SULFATE ION, 2,3-DIHYDROXY-1,4-DITHIOBUTANE, ... (5 entities in total)
• Functional Keywords: alpha-helix, pi-helix, signaling protein
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 17985.20

Authors

Spink, K.E.,Polakis, P.,Weis, W.I. (deposition date: 1999-12-06, release date: 2000-07-12, Last modification date: 2024-02-07)

Primary citation

Spink, K.E.,Polakis, P.,Weis, W.I.
Structural basis of the Axin-adenomatous polyposis coli interaction.
EMBO J., 19:2270-2279, 2000

PubMed 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.

PubMed: 10811618
DOI: 10.1093/emboj/19.10.2270

Experimental method

X-RAY DIFFRACTION (1.57 Å)