A model for the δ‐receptor‐bound conformation of enkephalin

FEBS Letters

Nikiforovich, G.V.¹  Balodis, J.¹ 

[1] Institute of Organic Synthesis, Latvian SSR Academy of Sciences, Aizkraukles 21, 226006 Riga, USSR

关键词: Energy calculation;    Enkephalin cycloanalog;    Receptor-bound conformation;    Receptor selectivity;   

DOI  :  10.1016/0014-5793(88)80882-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Sets of low-energy structures were determined by energy calculations for two cyclic analogues of enkephalin (Ek), [D-Pn⁵]-Ek and [D-Pn⁵]-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 Gly³ residue.

【 授权许可】

Unknown