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The three‐dimensional similarity between a dimeric antiparallel extended structure and a β‐turn folded form of enkephalin
Author(s) -
Doi Mitsunobu,
Tanaka Masayuki,
Ishida Toshimasa,
Inoue Masatoshi
Publication year - 1987
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(87)81503-x
Subject(s) - antiparallel (mathematics) , enkephalin , similarity (geometry) , turn (biochemistry) , chemistry , stereochemistry , crystallography , structural similarity , receptor , opioid , physics , biochemistry , computer science , artificial intelligence , quantum mechanics , magnetic field , image (mathematics)
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.