1upk
From Proteopedia
CRYSTAL STRUCTURE OF MO25 IN COMPLEX WITH A C-TERMINAL PEPTIDE OF STRAD
Overview
Mouse protein 25 alpha (MO25 alpha) is a 40-kDa protein that, together with the STE20-related adaptor-alpha (STRAD alpha) pseudo kinase, forms a regulatory complex capable of stimulating the activity of the LKB1 tumor suppressor protein kinase. The latter is mutated in the inherited Peutz-Jeghers cancer syndrome (PJS). MO25 alpha binds directly to a conserved Trp-Glu-Phe sequence at the STRAD alpha C terminus, markedly enhancing binding of STRAD alpha to LKB1 and increasing LKB1 catalytic activity. The MO25 alpha crystal structure reveals a helical repeat fold, distantly related to the Armadillo proteins. A complex with the STRAD alpha peptide reveals a hydrophobic pocket that is involved in a unique and specific interaction with the Trp-Glu-Phe motif, further supported by mutagenesis studies. The data represent a first step toward structural analysis of the LKB1-STRAD-MO25 complex, and suggests that MO25 alpha is a scaffold protein to which other regions of STRAD-LKB1, cellular LKB1 substrates or regulatory components could bind.
About this Structure
1UPK is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of MO25 alpha in complex with the C terminus of the pseudo kinase STE20-related adaptor., Milburn CC, Boudeau J, Deak M, Alessi DR, van Aalten DM, Nat Struct Mol Biol. 2004 Feb;11(2):193-200. Epub 2004 Jan 18. PMID:14730349 Page seeded by OCA on Sat May 3 11:32:19 2008
