Structural biology of human GPCR drugs and endogenous ligands - insights from NMR spectroscopy.

ABSTRACT: G protein-coupled receptors (GPCRs) represent the largest class of "druggable" proteins in the human genome. For more than a decade, crystal structures and, more recently, cryoEM structures of GPCR complexes have provided unprecedented insight into GPCR drug binding and cell signaling. Nevertheless, structure determination of receptors in complexes with weakly binding molecules or complex polypeptides remains especially challenging, including for hormones, many of which have so far eluded researchers. Nuclear magnetic resonance (NMR) spectroscopy has emerged as a promising approach to determine structures of ligands bound to their receptors and to provide insights into the dynamics of GPCR-bound drugs. The capability to investigate compounds with weak binding affinities has also been lever

SUBMITTER: Ferre G 

PROVIDER: S-EPMC7572649 | biostudies-literature | 2020 Aug

REPOSITORIES: biostudies-literature