Elucidating ligand-bound structures of membrane proteins using solid-state NMR spectroscopy.
Related Articles Elucidating ligand-bound structures of membrane proteins using solid-state NMR spectroscopy.
Curr Opin Struct Biol. 2019 Mar 20;57:103-109
Authors: Elkins MR, Hong M
Abstract
Magic-angle-spinning (MAS) solid-state NMR spectroscopy is a versatile technique to elucidate functionally important protein-ligand interactions in lipid membranes. Here, we review recent solid-state NMR studies of membrane protein interactions with cholesterol, lipids, transported substrates, and peptide ligands. These studies are conducted in synthetic or native lipid bilayers to provide an accurate environment for ligand binding. The solid-state NMR approaches include multinuclear detection to gain comprehensive structural information, distance measurements to locate ligand-binding sites, and dynamic nuclear polarization and 1H detection to enhance spectral sensitivity. These studies provide novel insights into the mechanisms of virus budding, virus entry into cells, transmembrane signaling, substrate transport, antibacterial action, and many other biological processes.
PMID: 30903830 [PubMed - as supplied by publisher]
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