TY - JOUR
T1 - Metadynamics simulations leveraged by statistical analyses and artificial intelligence-based tools to inform the discovery of G protein-coupled receptor ligands
AU - Salas-Estrada, Leslie
AU - Fiorillo, Bianca
AU - Filizola, Marta
N1 - Funding Information:
This work was supported by National Institutes of Health grant DA045473. The content is solely the responsibility of the authors and does not necessarily represent the official views of the National Institutes of Health. Computations in the Filizola lab are supported through the computational resources and staff expertise provided by Scientific Computing at the Icahn School of Medicine at Mount Sinai and are currently run on resources available through the Office of Research Infrastructure of the National Institutes of Health under award number S10OD026880. Acknowledgments
Publisher Copyright:
Copyright © 2022 Salas-Estrada, Fiorillo and Filizola.
PY - 2022/12/23
Y1 - 2022/12/23
N2 - G Protein-Coupled Receptors (GPCRs) are a large family of membrane proteins with pluridimensional signaling profiles. They undergo ligand-specific conformational changes, which in turn lead to the differential activation of intracellular signaling proteins and the consequent triggering of a variety of biological responses. This conformational plasticity directly impacts our understanding of GPCR signaling and therapeutic implications, as do ligand-specific kinetic differences in GPCR-induced transducer activation/coupling or GPCR-transducer complex stability. High-resolution experimental structures of ligand-bound GPCRs in the presence or absence of interacting transducers provide important, yet limited, insights into the highly dynamic process of ligand-induced activation or inhibition of these receptors. We and others have complemented these studies with computational strategies aimed at characterizing increasingly accurate metastable conformations of GPCRs using a combination of metadynamics simulations, state-of-the-art algorithms for statistical analyses of simulation data, and artificial intelligence-based tools. This minireview provides an overview of these approaches as well as lessons learned from them towards the identification of conformational states that may be difficult or even impossible to characterize experimentally and yet important to discover new GPCR ligands.
AB - G Protein-Coupled Receptors (GPCRs) are a large family of membrane proteins with pluridimensional signaling profiles. They undergo ligand-specific conformational changes, which in turn lead to the differential activation of intracellular signaling proteins and the consequent triggering of a variety of biological responses. This conformational plasticity directly impacts our understanding of GPCR signaling and therapeutic implications, as do ligand-specific kinetic differences in GPCR-induced transducer activation/coupling or GPCR-transducer complex stability. High-resolution experimental structures of ligand-bound GPCRs in the presence or absence of interacting transducers provide important, yet limited, insights into the highly dynamic process of ligand-induced activation or inhibition of these receptors. We and others have complemented these studies with computational strategies aimed at characterizing increasingly accurate metastable conformations of GPCRs using a combination of metadynamics simulations, state-of-the-art algorithms for statistical analyses of simulation data, and artificial intelligence-based tools. This minireview provides an overview of these approaches as well as lessons learned from them towards the identification of conformational states that may be difficult or even impossible to characterize experimentally and yet important to discover new GPCR ligands.
KW - GPCRs (G protein-coupled receptors)
KW - enhanced sampling
KW - machine learning
KW - metadynamics
KW - molecular dynamics simulation
UR - http://www.scopus.com/inward/record.url?scp=85145701237&partnerID=8YFLogxK
U2 - 10.3389/fendo.2022.1099715
DO - 10.3389/fendo.2022.1099715
M3 - Short survey
AN - SCOPUS:85145701237
SN - 1664-2392
VL - 13
JO - Frontiers in Endocrinology
JF - Frontiers in Endocrinology
M1 - 1099715
ER -