PDBsum entry 3qhe

Signaling protein/splicing

PDB id: 3qhe

Contents

Protein chains

323 a.a.

11 a.a.

Ligands

SER-TYR-GLU-GLY-TYR-GLU-GLY-TYR-TYR-SER

Waters ×262

PDB id:

3qhe

Name:

Signaling protein/splicing

Title:

Crystal structure of the complex between the armadillo repeat domain of adenomatous polyposis coli and the tyrosine-rich domain of sam68

Structure:

Adenomatous polyposis coli protein. Chain: a, c. Fragment: armadillo repeat domain, residues 396-732. Synonym: apc, protein apc, deleted in polyposis 2.5. Engineered: yes. Kh domain-containing, RNA-binding, signal transduction- associated protein 1. Chain: b, d. Fragment: tyrosine-rich domain, residues 365-419.

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: cell free synthsis. Other_details: e. Coli cell-free system. Other_details: e. Coli cell-free system

Resolution:

2.40Å R-factor: 0.189 R-free: 0.230

Authors:

E.C.J.Morishita,K.Murayama,M.Kato-Murayama,Y.Ishizuku-Katsura, Y.Tomabechi,T.Terada,N.Handa,M.Shirouzu,T.Akiyama,S.Yokoyama,Riken Structural Genomics/proteomics Initiative (Rsgi)

Key ref:

E.C.Morishita et al. (2011). 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. PubMed id: 22000517

Date:

25-Jan-11 Release date: 02-Nov-11

Protein chains

P25054  (APC_HUMAN) -  Adenomatous polyposis coli protein from Homo sapiens

Seq: 2843 a.a.

Struc: 323 a.a.

Protein chain

Q07666  (KHDR1_HUMAN) -  KH domain-containing, RNA-binding, signal transduction-associated protein 1 from Homo sapiens

Seq: 443 a.a.

Struc: 11 a.a.

Structure 19:1496-1508 (2011)

PubMed id: 22000517

Crystal structures of the armadillo repeat domain of adenomatous polyposis coli and its complex with the tyrosine-rich domain of Sam68.

E.C.Morishita, K.Murayama, M.Kato-Murayama, Y.Ishizuka-Katsura, Y.Tomabechi, T.Hayashi, T.Terada, N.Handa, M.Shirouzu, T.Akiyama, S.Yokoyama.

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.