Journal
CHEMISTRY & BIOLOGY
Volume 15, Issue 11, Pages 1207-1219Publisher
CELL PRESS
DOI: 10.1016/j.chembiol.2008.10.011
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Funding
- National Institutes of Health, National Institute on Drug Abuse [DA03934, DA000489, DA9158, DA3801]
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The extensive physiological influence of transmission through the CB2 cannabinoid receptor makes this G protein-coupled receptor (GPCR) a promising therapeutic target for treating neuropathic pain, inflammation, and immune disorders. However, there is little direct structural information pertaining to either GPCR or CB2-receptor ligand recognition and activation. The present work helps characterize experimentally the ligand-binding interactions of the human CB2 (hCB2) receptor. This study illustrates how our overall experimental approach, ligand-assisted protein structure (LAPS), affords direct determination of the requirements for ligand binding to the hCB2 receptor and discrimination among the binding motifs for ligands that activate therapeutically relevant GPCRs.
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