Structural and Biochemical Characterization of the Human Cyclophilin Family of Peptidyl-Prolyl Isomerases

Tara L Davis, John R Walker, Valérie Campagna-Slater, Patrick J Finerty, Ragika Paramanathan, Galina Bernstein, Farrell MacKenzie, Wolfram Tempel, Hui Ouyang, Wen Hwa Lee, Elan Z Eisenmesser and Sirano Dhe-Paganon

PLOS Biology, 2010, vol. 8, issue 7, 1-16

Abstract: Enhanced version: This article can also be viewed as an enhanced version in which the text of the article is integrated with interactive 3-D representations and animated transitions. Please note that a Web plugin is required to access this enhanced functionality. Instructions for the installation and use of the web plugin are available in Text S1. Author Summary: Cyclophilins are proteins that catalyze the isomerization of prolines, interconverting this structurally important amino acid between cis and trans isomers. Although there are 17 cyclophilins in the human genome, the function of most cyclophilin isoforms is unknown. At least some members of this protein family are of interest for clinically relevant drug design, as they are targets of the drug cyclosporin, which is used as an immunosuppressant to treat patients following organ transplantation. The absence of a comprehensive picture of the similarities and differences between the different members of this protein family precludes effective and specific drug design, however. In the current study we undertake such a global structure∶function analysis. Using biochemical, structural, and computational methods we characterize the human cyclophilin family in detail and suggest that there is a previously overlooked region of these enzymes that contributes significantly to isoform diversity. We propose that this region may represent an important target for isoform-specific drug design.

Date: 2010
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Persistent link: https://EconPapers.repec.org/RePEc:plo:pbio00:1000439

DOI: 10.1371/journal.pbio.1000439

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