1H, 13C and 15N backbone assignments of cyclophilin when bound to cyclosporin A (CsA) and preliminary structural characterization of the CsA binding site. |
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Authors: | P Neri R Meadows G Gemmecker E Olejniczak D Nettesheim T Logan R Simmer R Helfrich T Holzman J Severin |
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Institution: | Pharmaceutical Discovery Division, Abbott Laboratories, Abbott Park, IL 60064. |
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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. |
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