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A model for the δ‐receptor‐bound conformation of enkephalin
Author(s) -
Nikiforovich G.V.,
Balodis J.
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80882-2
Subject(s) - enkephalin , chemistry , residue (chemistry) , receptor , peptide , stereochemistry , opioid peptide , opioid receptor , biochemistry , opioid
Sets of low‐energy structures were determined by energy calculations for two cyclic analogues of enkephalin (Ek), [D‐P n 5 ]‐Ek and [D‐P n 5 ]‐Ek, possessing the highest specificity towards δ‐opioid receptors. Comparison of mutual spatial orientations of the α‐amino group and aromatic moieties of the Tyr and Phe residues permitted one to suggest a model for the δ‐receptor‐bound conformation of enkephalin‐related peptides. The model involves a pronounced γ‐like turn of the peptide backbone centred on the Gly 3 residue.