3AU3

Crystal structure of armadillo repeat domain of APC

Summary for 3AU3

• Entry DOI: 10.2210/pdb3au3/pdb
• Descriptor: Adenomatous polyposis coli protein (2 entities in total)
• Functional Keywords: armadillo repeat, signal transduction, signaling protein, structural genomics, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi
• Biological source: Homo sapiens (human)
• Cellular location: Cell junction, adherens junction: P25054
• Total number of polymer chains: 1
• Total formula weight: 38678.21

Authors

Murayama, K.,Kato-Murayama, M.,Terada, T.,Shirouzu, M.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2011-01-28, release date: 2011-11-02)

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 (2.1 Å)