Conformation of two non-immunosuppressive FK506 analogs when bound to FKBP by isotope-filtered NMR.

Petros AM, Kawai M, Luly JR, Fesik SW
FEBS Lett. 1992 308 (3): 309-14

PMID: 1380470 · DOI:10.1016/0014-5793(92)81300-b

The 3D structure of two unlabeled FK506 analogs, (R)- and (S)-[18-OH]ascomycin, when bound to [U-13C,15N]FKBP were determined by isotope-filtered 2D NMR experiments. The structures for the R and S isomers that bind tightly to FKBP but lack immunosuppressive 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.

MeSH Terms (13)

Binding Sites Calcineurin Calmodulin-Binding Proteins Carbon Isotopes Carrier Proteins Ligands Magnetic Resonance Spectroscopy Models, Molecular Molecular Conformation Phosphoprotein Phosphatases Protons Tacrolimus Tacrolimus Binding Proteins

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