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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
Author(s) -
Neri Placido,
Meadows Robert,
Gemmecker Gerd,
Olejniczak Edward,
Nettesheim David,
Logan Timothy,
Simmer Robert,
Helfrich Rosalind,
Holzman Thomas,
Severin Jean,
Fesik Stephen
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)81348-c
Subject(s) - heteronuclear molecule , cyclophilin , chemical shift , chemistry , cyclophilin a , stereochemistry , peptidylprolyl isomerase , binding site , cis trans isomerases , nuclear magnetic resonance spectroscopy , crystallography , biochemistry , biology , enzyme , microbiology and biotechnology , isomerase , gene
The 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.