Mapping the relationship between receptor dynamics and function in G protein–coupled receptors using molecular dynamics
G protein–coupled receptors (GPCRs) are key regulators of cellular signaling and major drug targets. Although X-ray crystallography and cryo-electron microscopy have provided high-resolution receptor structures, these static snapshots capture only a fraction of the conformational states underlying GPCR function. Molecular dynamics (MD) simulations complement experimental structures by enabling the mapping of receptor conformational landscapes and their relationship to functional outcomes. Large-scale simulation resources such as GPCRmd allow systematic exploration and comparison of GPCR motions across receptors and ligands. MD studies reveal transient conformational states, cryptic binding pockets, lipid- and water-mediated interactions, and allosteric communication networks that shape ligand recognition and the impact of signaling bias.
Authors
- Alejandro Peralta-García
- Jana Selent (ORCID: https://orcid.org/0000-0002-1844-4449)
- Adrián García‐Recio (ORCID: https://orcid.org/0000-0002-7143-9075)
- Anna Korda
- Natalia Acitores-Rich
Institutions
- Universitat Pompeu Fabra (ES)
Publication Details
- Journal
- Current Opinion in Structural Biology
- Published
- 2026-07-22
- DOI
- https://doi.org/10.1016/j.sbi.2026.103342
- Primary Topic
- Receptor Mechanisms and Signaling
- Type
- article
- Field-Weighted Citation Impact
- 0.00