NMR studies of [U-13C]cyclosporin A bound to human cyclophilin B.
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.
Pharmaceutical Discovery Division, Abbott Laboratories, Abbott Park, IL 60064.
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P
Neri
G
G
Gemmecker
L D
LD
Zydowsky
C T
CT
Walsh
S W
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Fesik
D000591:Amino Acid Isomerases / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure*; D001665:Binding Sites; D002352:Carrier Proteins / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure*; D016572:Cyclosporine / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D066298:In Vitro Techniques; D009682:Magnetic Resonance Spectroscopy; D008968:Molecular Conformation; D015394:Molecular Structure; D019696:Peptidylprolyl Isomerase; D011485:Protein Binding; D011487:Protein Conformation; D011994:Recombinant Proteins
D002352:Carrier Proteins; D011994:Recombinant Proteins; D016572:Cyclosporine; D000591:Amino Acid Isomerases; D019696:Peptidylprolyl Isomerase