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

✍ Scribed by Robert X. Xu; David Nettesheim; Edward T. Olejniczak; Robert Meadows; Gerd Gemmecker; Stephen W. Fesik

Publisher: Wiley (John Wiley & Sons)
Year: 1993
Tongue: English
Weight: 998 KB
Volume: 33
Category: Article
ISSN: 0006-3525
DOI: 10.1002/bip.360330404

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✦ Synopsis

Abstract

The ^1^H, ^13^C, and ^15^N 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‐^15^N] FKBP/ascomycin and [U‐^15^N, ^13^C] FKBP/ascomycin. In addition, from a preliminary analysis of two heteronuclear four‐dimensional data sets, ^3^J coupling constants, amide exchange data, and the differences between the C^α^ and C^β^ 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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