3QHE

Crystal structure of the complex between the armadillo repeat domain of adenomatous polyposis coli and the tyrosine-rich domain of Sam68

3QHE の概要

• エントリーDOI: 10.2210/pdb3qhe/pdb
• 分子名称: Adenomatous polyposis coli protein, KH domain-containing, RNA-binding, signal transduction-associated protein 1 (3 entities in total)
• 機能のキーワード: armadillo repeat superhelix, regulation of wnt signaling, tumor suppressor protein, adaptor protein, rna-binding protein, signaling protein-splicing protein complex, structural genomics, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi, signaling protein-splicing complex, signaling protein/splicing
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cell junction, adherens junction: P25054; Nucleus: Q07666
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 87991.04

構造登録者

Morishita, E.C.J.,Murayama, K.,Kato-Murayama, M.,Ishizuku-Katsura, Y.,Tomabechi, Y.,Terada, T.,Handa, N.,Shirouzu, M.,Akiyama, T.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (登録日: 2011-01-25, 公開日: 2011-11-02, 最終更新日: 2023-11-01)

主引用文献

Morishita, E.C.,Murayama, K.,Kato-Murayama, M.,Ishizuka-Katsura, Y.,Tomabechi, Y.,Hayashi, T.,Terada, T.,Handa, N.,Shirouzu, M.,Akiyama, T.,Yokoyama, S.
Crystal structures of the armadillo repeat domain of adenomatous polyposis coli and its complex with the tyrosine-rich domain of sam68
Structure, 19:1496-1508, 2011

PubMed Abstract: Adenomatous polyposis coli (APC) is a tumor suppressor protein commonly mutated in colorectal tumors. APC plays important roles in Wnt signaling and other cellular processes. Here, we present the crystal structure of the armadillo repeat (Arm) domain of APC, which facilitates the binding of APC to various proteins. APC-Arm forms a superhelix with a positively charged groove. We also determined the structure of the complex of APC-Arm with the tyrosine-rich (YY) domain of the Src-associated in mitosis, 68 kDa protein (Sam68), which regulates TCF-1 alternative splicing. Sam68-YY forms numerous interactions with the residues on the groove and is thereby fixed in a bent conformation. We assessed the effects of mutations and phosphorylation on complex formation between APC-Arm and Sam68-YY. Structural comparisons revealed different modes of ligand recognition between the Arm domains of APC and other Arm-containing proteins.

PubMed: 22000517
DOI: 10.1016/j.str.2011.07.013

実験手法

X-RAY DIFFRACTION (2.4 Å)