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NMR studies of [U‐ 13 C]cyclosporin A bound to human cyclophilin B
Author(s) -
Neri Placido,
Gemmecker Gerd,
Zydowsky Lynne D.,
Walsh Christopher T.,
Fesik Stephen W.
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)81258-a
Subject(s) - cypa , cyclophilin a , peptidylprolyl isomerase , cis trans isomerases , chemistry , chemical shift , cyclophilin , nuclear magnetic resonance spectroscopy , stereochemistry , isomerase , crystallography , biochemistry , biology , enzyme , microbiology and biotechnology , gene
NMR data ( 1 H and 13 C chemical shifts, NOEs) on [[U‐ 13 C]cyclosporin A bound to cyclophilin B were compared to previously published data on the [U‐ 13 C]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.