Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Isomerases / chemistry*
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Amino Acid Isomerases / metabolism
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Amino Acid Sequence
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Binding Sites
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Carbon Isotopes
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Carrier Proteins / chemistry*
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Carrier Proteins / metabolism
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Cloning, Molecular
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Cyclosporine / metabolism*
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Humans
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Hydrogen
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Magnetic Resonance Spectroscopy / methods
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Models, Molecular
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Molecular Sequence Data
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Nitrogen
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Peptidylprolyl Isomerase
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Protein Conformation
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Recombinant Proteins / chemistry
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Recombinant Proteins / metabolism
Substances
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Carbon Isotopes
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Carrier Proteins
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Recombinant Proteins
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Hydrogen
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Cyclosporine
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Amino Acid Isomerases
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Peptidylprolyl Isomerase
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Nitrogen