New receptor structures discovered to design drugs

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A team of researchers at USI has discovered the dimeric structural organisation of certain receptors among the principle drug targets in pharmacology. The findings have been published in the journal Nature Communications.

G-protein-coupled receptors (GPCRs), located in the cell membrane, control and regulate several vital functions in our body and are therefore elective molecular targets in pharmacology: more than one-third of drugs on the market have these receptors as "targets."

GPCRs form functional dimers, molecules composed of two distinct receptor units. In a recent paper published by Nature Communications ( doi:10.1038/s41467’023 -42082-z ), Professor Vittorio Limongelli of the Faculty of Biomedical Sciences with his team from the Euler Institute revealed the dimerization mechanism of the chemokine receptors CCR5 and CXCR4. The dimer structures of these receptors, first discovered in the study by Prof. Limongelli, exhibit important differences in their binding states for drugs and for proteins responsible for intracellular signal activation: dimerization, therefore, represents a fine allosteric mechanism for regulating receptor activity. This study paves the way for the design of drugs with improved pharmacological activity and reduced toxicity. Possible applications include research for new drugs in HIV, cancer, and immune-inflammatory diseases.




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