Hello Dr. Vipul Navadiya, I looked into this site because I wanted to understand more about the G protein receptor. I'm invested in CytoDyn, or CYDY on OTC exchange. I'm interested in a certain monoclonal antibody, Leronlimab, which binds to CCR5, which is a G protein receptor. The companies are calling it a CCR5 "blocker", but maybe it acts more like a binder. As it binds to the receptor very well with strong affinity. As it is a monoclonal antibody, it is larger, but I do not believe it affects any conformational changes in the g protein CCR5. Leronlimab has been shown very effective in knocking down HIV load and preventing AIDS in over 8 years of use in patients by working as an HIV entry inhibitor. In cancer, it prevents RANTES from binding to CCR5 so the Tumor cannot metastasize. It seems that Leronlimab is more of a RANTES or CCL5 blocker than a receptor blocker. What I don't understand is why when a ligand like Leronlimab binds to the CCR5 receptor, the same effects don't happen as when the RANTES ligand binds to the same CCR5 receptor? I don't know if you've studied Leronlimab, but its affinity for CCR5 is very strong, so I was curious, do you know if it knocks RANTES out of the receptor and replaces RANTES with itself? CCR5 is supposed to do with the kinetics of the cell, it is supposed to tell the cell where to travel. By doing so, inflammation somehow is reduced. Do you know anything about why the G proteins may be internalized to the interior of the cell and then they may later be re-expressed on the cell surfaces? Somehow in Long Haulers, these CCR5 G proteins are hardly expressed on the cell surfaces. Does RANTES have some thing to do with paralyzing the cells? It seems as if when these CCR5 receptors are bound with CCL5, the cell is found to be paralyzed, unable to do its job. It doesn't know what to do. It just sits there helpless. But when Leronlimab is added again, the CCR5 move back out to the cell surfaces and the cell comes back to life doing what it was supposed to do all the time.