1EMU
STRUCTURE OF THE AXIN RGS-HOMOLOGOUS DOMAIN IN COMPLEX WITH A SAMP REPEAT FROM APC
1EMU の概要
エントリーDOI | 10.2210/pdb1emu/pdb |
関連するPDBエントリー | 1DK8 |
分子名称 | AXIN, ADENOMATOUS POLYPOSIS COLI PROTEIN, GLYCEROL, ... (4 entities in total) |
機能のキーワード | rgs domain, signaling protein |
由来する生物種 | Homo sapiens (human) 詳細 |
細胞内の位置 | Cytoplasm : O15169 Cell junction, adherens junction : P25054 |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 17761.17 |
構造登録者 | |
主引用文献 | Spink, K.E.,Polakis, P.,Weis, W.I. Structural basis of the Axin-adenomatous polyposis coli interaction. EMBO J., 19:2270-2279, 2000 Cited by 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: 10811618DOI: 10.1093/emboj/19.10.2270 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.9 Å) |
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