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Conformation of two non‐immunosuppressive FK506 analogs when bound to FKBP by isotope‐filtered NMR
Author(s) -
Petros Andrew M.,
Kawai Megumi,
Luly Jay R.,
Fesik Stephen W.
Publication year - 1992
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(92)81300-b
Subject(s) - fkbp , chemistry , isotope , biochemistry , physics , nuclear physics
The 3D structure of two unlabeled FK506 analogs, ( R )‐ and ( S )‐[18‐OH]ascomycin, when bound to [U‐ 13 C, 14 N]FKBP were determined by isotope‐filtered 2D NMR experiments. The structures for the R and S isomers that bind tightly to FKBP but lack immunosuppresive activity are compared to each other and to the conformation of the potent immunosuppressant, ascomycin, when bound to FKBP. The results are interpreted in terms of calcineurin binding to the FKBP/ascomycin complex.