The existence of oligomeric assemblies of GPCRs has been confirmed by biochemical and biophysical studies including direct AFM imaging of rhodopsin in native membranes. The question is how they work together to transduce the signal into the cell and, further on, how the oligomeric state influences all aspects of their biological function. Crystallographic structure of rhodopsin revealed that its cytoplasmic surface is too small to bind the whole trimeric G protein and accommodate all interactions predicted from crosslinking data. According to our modeling, the trimeric transducin (G protein for rhodopsin) binds to rhodopsin tetramer.
We also revealed the modes of action of agonist/antagonist sensor in opioid receptors and investigated the central molecular switch in cannabinoid receptors (opioid and cannabinoid receptors are also GPCRs). We continue investigations of influence of ligands (agonists, antagonists and inverse agonists) on the receptor structure and the action of molecular switches in GPCRs.
ERNEST = European Research Network on Signal Transduction
The main scientific objective of the Action is to develop a common, comprehensive and holistic map of signal transduction that will advance development of pathway-specific chemical modulators. This unique and innovative goal will be realised by linking of a diverse group of researchers in the field through the networking activities funded by COST.
Our service GPCRM is completely reshaped, much faster, and user friendly. Now, it contains 3 main routes: Quick path (default), Long path, and High similarity (the fastest) for homology modeling of GPCRs. Currently, the service contains over 90 template structures. The updated version was recently published in NAR 2018, W1.