The three‐dimensional similarity between a dimeric antiparallel extended structure and a β‐turn folded form of enkephalin

FEBS Letters

Doi, Mitsunobu¹  Inoue, Masatoshi¹  Ishida, Toshimasa¹  Tanaka, Masayuki¹ 

[1] Osaka University of Pharmaceutical Sciences, 2-10-65 Kawai, Matsubara-City, Osaka 580, Japan

关键词: Enkephalin;    β-Turn conformation;    Extended dimeric conformation;    Energy calculation;    Conformational similarity;    Selectivity;   

DOI  :  10.1016/0014-5793(87)81503-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The three-dimensional similarity between two fundamental conformations, a dimeric antiparallel extended structure and a type I'β-turn folded form, of enkephalin was examined by computer graphic and empirical energy calculation methods. By the rotation of Tyr and Phe side chains, one half of the former structure could mimic the three-dimensional form of the latter without a large loss of conformational energy. This result provides a new idea for considering the conformation of enkephalin suitable for the multiple opioid receptors. The active conformation of enkephalin for μ- and δ-opioid receptors is discussed in the light of the present study.

【 授权许可】

Unknown