Structural basis for bifunctional peptide recognition at human delta-opioid receptor. IF 13.338

Bifunctional mu- and delta-opioid receptor (OR) ligands are potential therapeutic alternatives, with diminished side effects, to alkaloid opiate analgesics. We solved the structure of human delta-OR bound to the bifunctional delta-OR antagonist and mu-OR agonist tetrapeptide H-Dmt-Tic-Phe-Phe-NH2 (DIPP-NH2) by serial femtosecond crystallography, revealing a cis-peptide bond between H-Dmt and Tic. The observed receptor-peptide interactions are critical for understanding of the pharmacological profiles of opioid peptides and for development of improved analgesics.

Jaar van publicatie:2015

Trefwoorden:SERIAL FEMTOSECOND CRYSTALLOGRAPHY; MU AGONIST/DELTA ANTAGONIST; POTENT; TOLERANCE; DEPENDENCE; MORPHINE; BOND; DMT

CSS-citation score:3

Toegankelijkheid:Closed