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The 3D structure of a cyclosporin analogue in water is nearly identical to the cyclophilin‐bound cyclosporin conformation
Author(s) -
Wenger Roland M.,
France Julien,
Bovermann Günter,
Walliser Louis,
Widmer Armin,
Widmer Hans
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)80149-5
Subject(s) - cyclophilin , chemistry , chloroform , cyclophilin a , cyclosporins , stereochemistry , solvent , derivative (finance) , polar , peptidylprolyl isomerase , crystallography , isomerase , biochemistry , organic chemistry , biology , transplantation , enzyme , microbiology and biotechnology , medicine , physics , surgery , astronomy , financial economics , economics , gene
The conformation of [ d ‐MeSer 3 ‐ d ‐Ser‐( O ‐Gly 8 ]CS, a water soluble cyclosporin derivative, has been determined in (D 6 )DMSO and in water using NMR. In these polar solvents the conformation is identical and very similar to the structure found in the cyclophilin‐cyclosporin complex. However, it differs significantly from its conformation in deuterated chloroform. This demonstrates unambiguously that the large structure change is induced primarily by the polar solvent rather than by complex formation with cyclophilin.