H-1, C-13, AND N-15 ASSIGNMENTS AND SECONDARY STRUCTURE OF THE FK506 BINDING-PROTEIN WHEN BOUND TO ASCOMYCIN

被引：31

作者：

XU, RX ^{[1
]}

NETTESHEIM, D ^{[1
]}

OLEJNICZAK, ET ^{[1
]}

MEADOWS, R ^{[1
]}

GEMMECKER, G ^{[1
]}

FESIK, SW ^{[1
]}

机构：

[1] ABBOTT LABS,DIV PHARMACEUT DISCOVERY,ABBOTT PK,IL 60064

来源：

BIOPOLYMERS | 1993年 / 33卷 / 04期

关键词：

D O I：

10.1002/bip.360330404

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The H-1, C-13, and N-15 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-N-15]FKBP/ascomycin and [U-N-15, C-13]FKBP/ascomycin. In addition, from a preliminary analysis of two heteronuclear four-dimensional data sets, 3J(HN,Halpha) 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.

引用

页码：535 / 550

页数：16

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