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1 H, 13 C, and 15 N assignments and secondary structure of the FK506 binding protein when bound to ascomycin
Author(s) -
Xu Robert X.,
Nettesheim David,
Olejniczak Edward T.,
Meadows Robert,
Gemmecker Gerd,
Fesik Stephen W.
Publication year - 1993
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360330404
Subject(s) - fkbp , heteronuclear molecule , chemistry , amide , stereochemistry , crystallography , nuclear magnetic resonance spectroscopy , biochemistry
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 H N ,H αcoupling 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.