title: A model for the delta-receptor-bound conformation of enkephalin.
abstract: Sets of low-energy structures were determined by energy calculations for two cyclic analogues of enkephalin (Ek), [D-Pen2, D-Pen5]-Ek and [D-Pen2, L-Pen5]-Ek, possessing the highest specificity towards delta-opioid receptors. Comparison of mutual spatial orientations of the alpha-amino group and aromatic moieties of the Tyr and Phe residues permitted one to suggest a model for the delta-receptor-bound conformation of enkephalin-related peptides. The model involves a pronounced gamma-like turn of the peptide backbone centred on the Gly3 residue.
authors.affiliation: Institute of Organic Synthesis, Latvian SSR Academy of Sciences, Riga.
authors.forename: G V
authors.initials: GV
authors.lastname: Nikiforovich
authors.forename: J
authors.initials: J
authors.lastname: Balodis
mesh_terms: D002151:Calorimetry; D004745:Enkephalins / Q000378:metabolism*; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation; D011957:Receptors, Opioid / Q000378:metabolism*; D017465:Receptors, Opioid, delta; D013329:Structure-Activity Relationship
chemical_list: D004745:Enkephalins; D011957:Receptors, Opioid; D017465:Receptors, Opioid, delta