1upk

From Proteopedia

Revision as of 15:03, 5 November 2007

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 with MES as ligand. Structure known Active Site: AC1. 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

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