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Solution structure of FK506 bound to FKBP‐12
Author(s) -
Lepre Christopher A.,
Thomson John A.,
Moore Jonathan M.
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)80292-o
Subject(s) - fkbp , intermolecular force , crystallography , chemistry , ligand (biochemistry) , crystal structure , molecular dynamics , inverse , biophysics , molecule , stereochemistry , receptor , geometry , computational chemistry , biochemistry , biology , mathematics , organic chemistry
The complex of the immunosuppressant FK506 bound to FKBP‐12 has been studied in solution using 1 H and inverse‐detected 13 C NMR methods. The resonances of bound, 13 C‐labelled FK506 were assigned and a set of 66 intraligand NOE distance restraints were used to calculate the structure of the bound ligand by distance geometry and restrained molecular dynamics methods. The structure of bound FK506 in solution closely resembles that seen in the X‐ray structure [17], except for the allyl region. The differences reflect the influence of intermolecular crystal contacts and have implications for interpretation of the interaction of the FK506/FKBP complex with its putative biological receptor.