TI - 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

DOIResolve DOI: http://doi.org/10.1016/j.bbrc.2006.07.036
AuthorSearch for: ; Search for: ; Search for:
TypeArticle
Volume347
Issue4
Pages11451150; # of pages: 6
SubjectMutation; Peptide Fragments; pha; Protein; Protein-Serine-Threonine Kinases; Proteins; Saccharomyces cerevisiae; Yeast
AbstractIn 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
Publication date
AffiliationNRC Biotechnology Research Institute; National Research Council Canada
Peer reviewedNo
NRC number47517
NPARC number3539790
Export citationExport as RIS
Report a correctionReport a correction
Record identifier403d62ca-b41a-4be9-8bee-91a8d2fc656e
Record created2009-03-01
Record modified2016-05-09
Bookmark and share
  • Share this page with Facebook (Opens in a new window)
  • Share this page with Twitter (Opens in a new window)
  • Share this page with Google+ (Opens in a new window)
  • Share this page with Delicious (Opens in a new window)