A Lipid Pathway for Ligand Binding Is Necessary for a Cannabinoid G Protein-coupled Receptor
Open Access
- 1 June 2010
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 285 (23) , 17954-17964
- https://doi.org/10.1074/jbc.m109.041590
Abstract
No abstract availableKeywords
This publication has 73 references indexed in Scilit:
- Concerted Interconversion between Ionic Lock Substates of the β2 Adrenergic Receptor Revealed by Microsecond Timescale Molecular DynamicsBiophysical Journal, 2010
- Location, Structure, and Dynamics of the Synthetic Cannabinoid Ligand CP-55,940 in Lipid BilayersBiophysical Journal, 2009
- Identification of two distinct inactive conformations of the β 2 -adrenergic receptor reconciles structural and biochemical observationsProceedings of the National Academy of Sciences, 2009
- Two protonation switches control rhodopsin activation in membranesProceedings of the National Academy of Sciences, 2008
- Structure of a β1-adrenergic G-protein-coupled receptorNature, 2008
- Sequence of late molecular events in the activation of rhodopsinProceedings of the National Academy of Sciences, 2007
- High-Resolution Crystal Structure of an Engineered Human β 2 -Adrenergic G Protein–Coupled ReceptorScience, 2007
- All-Atom Empirical Potential for Molecular Modeling and Dynamics Studies of ProteinsThe Journal of Physical Chemistry B, 1998
- VMD: Visual molecular dynamicsJournal of Molecular Graphics, 1996
- Specific Tryptophan UV-Absorbance Changes Are Probes of the Transition of Rhodopsin to Its Active StateBiochemistry, 1996