LOV2GIVe allows to activate Gi proteins non-invasively with innocuous blue light based on a design principle unrelated to light-activated GPCRs (metazoan opsins), thereby expanding the range of potential experimental applications.
Hydrogen-Deuterium exchange experiments show that Ric-8A induces similar dynamic changes in the structure of Gα as G protein-coupled receptors, yet protects a larger surface of the nucleotide-binding Ras domain.
The structure of a light-sensitive G protein-coupled receptor in complex with a Gi-protein heterotrimer provides a structural foundation for the role of the receptor C-terminal tail in scaffolding and signaling.
Combining powerful simulation methods uncovers the structural and dynamical changes driving G protein activation in atomic detail, revealing the allosteric network that triggers GDP release and reconciling diverse experimental data.
The maize CLAVATA receptor, FEA2, functions in the perception of two different ligands, and remarkably that signaling from these different inputs is differentiated by the receptor interacting with two different downstream components.