A model for the delta-receptor-bound conformation of enkephalin.
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.
Nikiforovich
G V
GV
Institute of Organic Synthesis, Latvian SSR Academy of Sciences, Riga.
Balodis
J
J
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
D004745:Enkephalins; D011957:Receptors, Opioid; D017465:Receptors, Opioid, delta