![]() By analyzing the conformational changes in 234 structures from 45 class A GPCRs, we discovered a common GPCR activation pathway comprising of 34 residue pairs and 35 residues. Here, we report a framework to quantify conformational changes. ![]() ![]() However, what leads to TM6 movement and the key residue level changes of this movement remain less well understood. GPCR activation is an allosteric process that couples agonist binding to G-protein recruitment, with the hallmark outward movement of transmembrane helix 6 (TM6). Understanding receptor activation mechanism is critical for discovering novel therapeutics since about one-third of all marketed drugs target members of this family. ![]() Class A G-protein-coupled receptors (GPCRs) influence virtually every aspect of human physiology.
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