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Aranda-Garcia, D.

Publications and source records attributed to Aranda-Garcia, D..

2 recordsLinked to original sources

Integrative Biophysical Illumination of the 3D GPCRome Dynamics

Achieving high-resolution insights into protein dynamics remains a major challenge, particularly for membrane proteins such as G protein-coupled receptors (GPCRs) - a highly dynamic class of cell surface receptors and key drug targets. Here, we present an integrative strategy that bridges computational and experimental biophysical methods for probing protein dynamics. To illustrate its potential, we developed GPCRmd-NMR, a platform that synergistically combines molecular dynamics (MD) simulations with high-resolution nuclear magnetic resonance (NMR) spectroscopy across the 3D GPCRome. The resulting dataset maps over 20 billion NMR signals to more than 7 million conformational snapshots of GPCRs, enabling structure-resolved analysis at an unprecedented scale. Application across multiple GPCRs provides access to previously underexplored functional GPCR dynamics, receptor states, and sites, including microswitches and hidden ligand entrance gateways. Our integrated framework offers a powerful solution to long-standing challenges faced by both experimental and computational researchers. To support broad accessibility, GPCRmd-NMR is available as an open-access, web-based framework equipped with user-friendly analysis tools (https://www.gpcrmd.org/gpcrmd-nmr-tool) and is readily applicable to other dynamic protein families beyond GPCRs and other types of biophysical data.

bioinformatics↗

GPCRmd uncovers the dynamics of the 3D-GPCRome

G protein-coupled receptors (GPCRs) are involved in numerous physiological processes and are the most frequent targets of approved drugs. The explosion in the number of new 3D molecular structures of GPCRs (3D-GPCRome) during the last decade has greatly advanced the mechanistic understanding and drug design opportunities for this protein family. While experimentally-resolved structures undoubtedly provide valuable snapshots of specific GPCR conformational states, they give only limited information on their flexibility and dynamics associated with function. Molecular dynamics (MD) simulations have become a widely established technique to explore the conformational landscape of proteins at an atomic level. However, the analysis and visualization of MD simulations requires efficient storage resources and specialized software, hence limiting the dissemination of these data to specialists in the field. Here we present the GPCRmd (http://gpcrmd.org/), an online platform that incorporates web-based visualization capabilities as well as a comprehensive and user-friendly analysis toolbox that allows scientists from different disciplines to visualize, analyse and share GPCR MD data. GPCRmd originates from a community-driven effort to create the first open, interactive, and standardized database of GPCR MD simulations. We demonstrate the power of this resource by performing comparative analyses of multiple GPCR simulations on two mechanisms critical to receptor function: internal water networks and sodium ion interaction.

biophysics↗