X-ray structure of a decameric cyclophilin-cyclosporin crystal complex
Article Abstract:
X-ray crystallography was used to determine the crystal structure of the cyclophilin-cyclosporin complex. It is an asymmetric pentameter structure consisting of cyclophilin-cyclosporin complexes. A high quality electron density map was obtained that clearly shows the five independent cylosporin molecules. Previous nuclear magnetic resonance (NMR) and X-ray studies are confirmed. These results should aid in understanding the immunosuppressant function of cyclosporin and the design of analogous drugs.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1993
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NMR structure and mutagenesis of the Fas (APO-1/CD95) death domain
Article Abstract:
Nuclear magnetic resonance spectroscopy and protein-binding assay were done to study the solution structure and function of Fas, a cytokine receptor which mediates programmed cell death. The results revealed that the death domain of the receptor consists of six antiparallel, amphipathic alpha-helices that are arranged in a novel fold. Fas was also found to bind to another death-domain-containing signalling protein, FADD via a hydrophobic site composed of alpha-5 and alpha-6 helices.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1996
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Solution structure of the cyclosporin A/cyclophilin complex by NMR
Article Abstract:
Heteronuclear three-dimensional nuclear magnetic resonance (NMR) spectroscopy was used to determine the solution structure of the cyclosporin A/cyclophilin complex. The structure of the complex differs considerably from previous models. Knowledge of this structure adds to that for the uncomplexed molecules and may shed light on the function of cyclosporin A as an immunosuppressant.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1993
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