Fig. 4: Structural dynamics analysis of mGlu2 dimers in response to orthosteric and allosteric ligands.
a–c Representative τDA vs. E histogram for mGlu2 dimers in the absence (Apo) or presence of Glu or Glu + BINA. For the Apo receptors, the major population deviates from the “Static FRET” line (yellow), indicating conformational dynamics at the submillisecond time scale. The addition of Glu stabilizes the VFT in an ensemble of low FRET conformations with less flexibility, an effect that is reinforced by the allosteric modulator BINA. d–f Time window analysis for different integration times (from 0.2–1 ms) reveals large conformational flexibility of the Apo VFT at 200–600 µs timescales, which is strongly restricted when bound to orthosteric agonist and allosteric modulator. The number of data points used varied from 2183-1640-901 (d–f respectively, 200 µs) to 14082-13132-13269 (1 ms) g–j Schematic representation of the major species observed in all cases, with the timescales of the transition between them. Black and blue dots represent Glu and BINA, respectively. Source data of panels a–f are provided upon request.
