3QHE

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

Summary for 3QHE

• Entry DOI: 10.2210/pdb3qhe/pdb
• Descriptor: Adenomatous polyposis coli protein, KH domain-containing, RNA-binding, signal transduction-associated protein 1 (3 entities in total)
• Functional Keywords: 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
• Biological source: Homo sapiens (human); More
• Cellular location: Cell junction, adherens junction: P25054; Nucleus: Q07666
• Total number of polymer chains: 4
• Total formula weight: 87991.04

Authors

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) (deposition date: 2011-01-25, release date: 2011-11-02, Last modification date: 2023-11-01)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.4 Å)