G-protein diseases furnish a model for the turn-on switch
- 1 July 1998
- journal article
- progress
- Published by Springer Nature in Nature
- Vol. 394 (6688) , 35-38
- https://doi.org/10.1038/27831
Abstract
How does a trimeric G protein on the inside of a cell membrane respond to activation by a transmembrane receptor? G-protein mutations in patients with hypertension and inherited endocrine disorders enhance or block signals from stimulated receptors. In combination with three-dimensional crystal structures and results from biochemical experiments, the phenotypes produced by these mutations suggest a model for the molecular activation mechanism that relays hormonal and sensory signals transmitted by many transmembrane receptors.Keywords
This publication has 38 references indexed in Scilit:
- The Many Faces of G Protein SignalingJournal of Biological Chemistry, 1998
- An alpha-carbon template for the transmembrane helices in the rhodopsin family of G-protein-coupled receptors 1 1Edited by R. HuberJournal of Molecular Biology, 1997
- G PROTEIN MECHANISMS: Insights from Structural AnalysisAnnual Review of Biochemistry, 1997
- How receptors talk to trimeric G proteinsCurrent Opinion in Cell Biology, 1997
- The 2.0 Å crystal structure of a heterotrimeric G proteinNature, 1996
- Photoactivated state of rhodopsin and how it can formBiophysical Chemistry, 1995
- The family of G‐protein‐coupled receptorsThe FASEB Journal, 1995
- Interaction of rhodopsin with the G‐protein, transducinBioEssays, 1993
- The GTPase superfamily: conserved structure and molecular mechanismNature, 1991
- The GTPase superfamily: a conserved switch for diverse cell functionsNature, 1990