1 H, 13 C and 15 N backbone assignments of cyclophilin when bound to cyclosporin A (CsA) and preliminary structural characterization of the CsA binding site
1991; Wiley; Volume: 294; Issue: 1-2 Linguagem: Inglês
10.1016/0014-5793(91)81348-c
ISSN1873-3468
AutoresPlacido Neri, Robert Meadows, Gerd Gemmecker, Edward T. Olejniczak, David G. Nettesheim, Timothy M. Logan, Robert L. Simmer, Rosalind Helfrich, Thomas F. Holzman, Jean M. Severin, Stephen W. Fesik,
Tópico(s)Calpain Protease Function and Regulation
ResumoThe backbone 1 H, 13 C and 15 N chemical shifts of cyclophilin (CyP) when bound to cyclosporin A (CsA) have been assigned from heteronuclear two‐ and three‐dimensional NMR experiments involving selectively 15 N‐ and uniformly 15 N‐ and 15 N, 13 C‐labeled cyclophilin. From an analysis of the 1 H and 15 N 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.
Referência(s)