The conformation of cyclosporin a bound to cyclophilin is altered (once again) following binding to calcineurin: an analysis of receptor-ligand-receptor interactions

Michael K. Rosen; Peter J. Belshaw; David G. Alberg; Stuart L. Schreiber

doi:10.1016/S0960-894X(00)80405-9

The conformation of cyclosporin a bound to cyclophilin is altered (once again) following binding to calcineurin: an analysis of receptor-ligand-receptor interactions

Michael K. Rosen, Peter J. Belshaw, David G. Alberg, Stuart L. Schreiber

Research output: Contribution to journal › Article › peer-review

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Abstract

Analyses of the complexation of cyclosporin A (CsA) by cyclophilin and the unusual properties of MeBm₂t¹-CsA lead us to propose a conformational change upon binding of the cyclophilin-CsA complex to the protein phosphatase, calcineurin.

Original language	English (US)
Pages (from-to)	747-753
Number of pages	7
Journal	Bioorganic and Medicinal Chemistry Letters
Volume	2
Issue number	7
DOIs	https://doi.org/10.1016/S0960-894X(00)80405-9
State	Published - Jul 1992

ASJC Scopus subject areas

Biochemistry
Molecular Medicine
Molecular Biology
Pharmaceutical Science
Drug Discovery
Clinical Biochemistry
Organic Chemistry

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10.1016/S0960-894X(00)80405-9

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The conformation of cyclosporin a bound to cyclophilin is altered (once again) following binding to calcineurin: an analysis of receptor-ligand-receptor interactions. / Rosen, Michael K.; Belshaw, Peter J.; Alberg, David G. et al.
In: Bioorganic and Medicinal Chemistry Letters, Vol. 2, No. 7, 07.1992, p. 747-753.

Research output: Contribution to journal › Article › peer-review

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abstract = "Analyses of the complexation of cyclosporin A (CsA) by cyclophilin and the unusual properties of MeBm2t1-CsA lead us to propose a conformational change upon binding of the cyclophilin-CsA complex to the protein phosphatase, calcineurin.",

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The conformation of cyclosporin a bound to cyclophilin is altered (once again) following binding to calcineurin: an analysis of receptor-ligand-receptor interactions

Abstract

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