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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

DOITrouver le DOI : https://doi.org/10.1016/j.bbrc.2006.07.036
AuteurRechercher : ; Rechercher : 1; Rechercher : 1
Affiliation
  1. Conseil national de recherches Canada. Institut de recherche en biotechnologie du CNRC
FormatTexte, Article
SujetMutation; Peptide Fragments; pharmaceutical; Protein; Protein-Serine-Threonine Kinases; Proteins; Saccharomyces cerevisiae; Yeast
Résumé
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
Date de publication
Numéro du CNRC47517
Numéro NPARC3539790
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Identificateur de l’enregistrement403d62ca-b41a-4be9-8bee-91a8d2fc656e
Enregistrement créé2009-03-01
Enregistrement modifié2020-04-22

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