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8. 1H, 13C, and 15N assignments and secondary structure of the FK506 binding protein when bound to ascomycin.

Author

Xu RX, Nettesheim D, Olejniczak ET, Meadows R, Gemmecker G, and Fesik SW

Subjects
Amino Acid Sequence, Carrier Proteins metabolism, Humans, In Vitro Techniques, Magnetic Resonance Spectroscopy, Molecular Sequence Data, Protein Structure, Secondary, Recombinant Proteins chemistry, Recombinant Proteins metabolism, Tacrolimus analogs & derivatives, Tacrolimus Binding Proteins, Carrier Proteins chemistry, Tacrolimus metabolism
Abstract

The 1H, 13C, and 15N resonances of FKBP when bound to the immunosuppressant, ascomycin, were assigned using a computer-aided analysis of heteronuclear double and triple resonance three-dimensional nmr spectra of [U-15N]FKBP/ascomycin and [U-15N,13C]FKBP/ascomycin. In addition, from a preliminary analysis of two heteronuclear four-dimensional data sets, 3JHN,H alpha coupling constants, amide exchange data, and the differences between the C alpha and C beta chemical shifts of FKBP to random coil values, the secondary structure of FKBP when bound to ascomycin was determined. The secondary structure of FKBP when bound to ascomycin in solution closely resembled the x-ray structure of the FKBP/FK506 complex but differed in some aspects from the structure of uncomplexed FKBP in solution.

Published
1993
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