1H,13C and 15N backbone assignments of cyclophilin when bound to cyclosporin A (CsA) and preliminary structural characterization of the CsA binding site

FEBS Letters

Meadows, Robert¹  Neri, Placido¹  Severin, Jean¹  Helfrich, Rosalind¹  Olejniczak, Edward¹  Logan, Timothy¹  Holzman, Thomas¹  Simmer, Robert¹  Gemmecker, Gerd¹  Fesik, Stephen¹  Nettesheim, David¹ 

[1] Pharmaceutical Discovery Division, Abbott Laboratories, Abbott Park, IL 60064, USA

关键词: Cyclophilin;    Cyclosporin A;    NMR;    CyP;    cyclophilin;    CsA;    cyclosporin A;    FKBP;    FK506 binding protein;    NOE;    nuclear Overhauser effect;    HSQC;    heteronuclear single quantum correlation;    NOESY;    nuclear Overhauser effect spectroscopy;    TOCSY;    total correlation spectroscopy;    HMQC;    heteronuclear multiple quantum correlation;   

DOI  :  10.1016/0014-5793(91)81348-C

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The backbone ¹H, ¹³C and ¹⁵N chemical shifts of cyclophilin (CyP) when bound to cyclosporin A (CsA) have been assigned from heteronuclear two- and three-dimensional NMR experiments involving selectively ¹⁵N- and uniformly ¹⁵N- and ¹⁵N,¹³C-labeled cyclophilin. From an analysis of the ¹H and ¹⁵N chemical shifts of CyP that change upon binding to CsA and from CyP/CsA NOEs, we have determined the regions of cyclophilin involved in binding to CsA.

【 授权许可】

Unknown