Neri P, Gemmecker G, Zydowsky L D, Walsh C T, Fesik S W
Pharmaceutical Discovery Division, Abbott Laboratories, Abbott Park, IL 60064.
FEBS Lett. 1991 Sep 23;290(1-2):195-9. doi: 10.1016/0014-5793(91)81258-a.
NMR data (1H and 13C chemical shifts, NOEs) on [U-13C]cyclosporin A bound to cyclophilin B were compared to previously published data on the [U-13C]CsA/CyPA complex [Fesik et al., (1991) Biochemistry 30, 6574-6583]. Despite only 64% sequence identity between CyPA and CyPB, the conformation and active site environment of CsA when bound to CyPA and CyPB are nearly identical as judged by the similarity of the NMR data.
将与亲环蛋白B结合的[U-13C]环孢素A的核磁共振数据（1H和13C化学位移、核Overhauser效应）与之前发表的关于[U-13C]环孢素A/亲环蛋白A复合物的数据[费西克等人，（1991年）《生物化学》30卷，6574 - 6583页]进行了比较。尽管亲环蛋白A和亲环蛋白B之间只有64%的序列同一性，但根据核磁共振数据的相似性判断，环孢素A与亲环蛋白A和亲环蛋白B结合时的构象和活性位点环境几乎相同。
