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Biochem Biophys Res Commun


Title:An NMR-based identification of a peptide fragment from the beta-subunit of a G-protein showing specific interactions with the GBB domain of the Ste20 kinase in budding yeast
Author(s):Bhattacharjya S; Gingras R; Xu P;
Address:"School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551, Singapore. surajit@ntu.edu.sg"
Journal Title:Biochem Biophys Res Commun
Year:2006
Volume:20060717
Issue:4
Page Number:1145 - 1150
DOI: 10.1016/j.bbrc.2006.07.036
ISSN/ISBN:0006-291X (Print) 0006-291X (Linking)
Abstract:"In mitogen-activated protein kinase (MAPK) cascades of budding yeast, pheromone-induced mating signal is transmitted by interactions between the beta-subunit of a G-protein (G-beta) and the G-beta binding (GBB) domain of Ste20 kinase. Previously, mutational analyses of the beta-subunit of G-protein had identified two critical mutations which abrogate binding of the GBB domain of Ste20. In this work, we have identified, by use of NMR spectroscopy, a peptide fragment from the G-beta that shows specific interactions with the isolated GBB domain of Ste20. A model structure of the Ste20/G-beta complex reveals that the interface of the hetero-complex may be sustained by parallel orientation of two potentially interacting helical segments that are further stabilized by ionic, hydrogen bond, and helix macro-dipole interactions"
Keywords:"Amino Acid Sequence Binding Sites/physiology GTP-Binding Protein beta Subunits/*metabolism Intracellular Signaling Peptides and Proteins MAP Kinase Kinase Kinases MAP Kinase Signaling System/physiology Models, Molecular Molecular Sequence Data Nuclear Mag;"
Notes:"MedlineBhattacharjya, Surajit Gingras, Richard Xu, Ping eng Research Support, Non-U.S. Gov't 2006/07/28 Biochem Biophys Res Commun. 2006 Sep 8; 347(4):1145-50. doi: 10.1016/j.bbrc.2006.07.036. Epub 2006 Jul 17"

 
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