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Similarity of Ca 2+ ‐bound conformations of morphine and Met‐enkephalin: A computational study
Author(s) -
Zhorov Boris S.,
Ananthanarayanan Vettai S.
Publication year - 1994
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(94)01071-4
Subject(s) - enkephalin , morphine , similarity (geometry) , chemistry , stereochemistry , opioid , biochemistry , pharmacology , biology , computer science , receptor , artificial intelligence , image (mathematics)
The conformations of the free and Ca 2+ ‐bound forms of morphine and Met‐enkephalin were compared based on an earlier proposal that extracellular Ca 2+ may dictate the bioactive conformations of peptide hormones and drugs. A Monte Carlo with energy minimization method was used to calculate Met‐enkephalin in the absence and presence of Ca 2+ . The Ca 2+ ‐bound conformation of Met‐enkephalin was found to have an overall shape that matched well with that of morphine. In contrast, the uncomplexed Met‐enkephalin did not have such a match. The data suggest that a ternary association of μ‐receptor, its ligands and Ca 2+ may be an initial process in the signal transduction mechanism of opioid peptides.