G Protein-coupled Receptor (GPCR) Reconstitution and Labeling for Solution Nuclear Magnetic Resonance (NMR) Studies of the Structural Basis of Transmembrane Signaling

• Published in: Molecules (Basel, Switzerland) Vol. 27; no. 9; p. 2658
• Main Authors: Ge, Haoyi, Wang, Huixia, Pan, Benxun, Feng, Dandan, Guo, Canyong, Yang, Lingyun, Liu, Dongsheng, Wüthrich, Kurt
• Format: Journal Article
• Language: English
• Published: Switzerland MDPI AG 20.04.2022; MDPI
• Subjects: 19F-NMR; Amino acids; amino-acid-specific NMR labeling; Aqueous solutions; Binding sites; Drug development; Experiments; Fluorine; G protein-coupled receptors; Humans; in-membrane chemical modification; Kinases; Labeling; Ligands; Lipids; Magnetic Resonance Spectroscopy - methods; membrane mimetics; Membrane proteins; Molecular Conformation; Nanoparticles; NMR; NMR spectroscopy; Nuclear magnetic resonance; Prescription drugs; Proteins; Receptors, G-Protein-Coupled - metabolism; Resonance; Review; Signal Transduction; Spectroscopy; stable-isotope labeling; in-membrane chemical modification; 19F-NMR; sequence-specific NMR labeling; G protein-coupled receptors; membrane mimetics; stable-isotope labeling; amino-acid-specific NMR labeling
• ISSN: 1420-3049; 1420-3049
• DOI: 10.3390/molecules27092658

G protein-coupled receptors (GPCRs) are a large membrane protein family found in higher organisms, including the human body. GPCRs mediate cellular responses to diverse extracellular stimuli and thus control key physiological functions, which makes them important targets for drug design. Signaling by GPCRs is related to the structure and dynamics of these proteins, which are modulated by extrinsic ligands as well as by intracellular binding partners such as G proteins and arrestins. Here, we review some basics of using nuclear magnetic resonance (NMR) spectroscopy in solution for the characterization of GPCR conformations and intermolecular interactions that relate to transmembrane signaling.