1H, 13C,and 15N assignments and secondary structure of the FK506 binding protein when bound to ascomycin |
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Authors: | Robert X. Xu David Nettesheim Edward T. Olejniczak Robert Meadows Gerd Gemmecker Stephen W. Fesik |
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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, 3J coupling constants, amide exchange data, and the differences between the Cα and Cβ 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. © 1993 John Wiley & Sons, Inc. |
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