Leipzig and Shanghai Scientists Solve the Cryo-EM Structure of Neuropeptide Y Bound to Its Y5 Receptor, a Target for Cachexia and Cancer
Researchers at Leipzig University and the Shanghai Institute of Materia Medica reported in Angewandte Chemie on October 28, 2026 the cryo-electron microscopy structure of the neuropeptide Y5 receptor bound to neuropeptide Y and its G protein. The structure shows features of the receptor's outer surface that help it recognize the peptide and how the tail end of neuropeptide Y binds, backed by mutation tests with neuropeptide Y and a selective Y5 agonist. The authors say the lack of structural data had slowed drug development for the Y5 receptor, which is studied as a target in cachexia and cancer.