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  1. 1 Biotechnologia

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  1. 1 2002

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  1. 1 Nuc K.

  2. 1 Slomski R.

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Structure and function of cyclophilins

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Nuc K., Slomski R.
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Cyclophilins (CyPs) constitute a large class of highly conserved, ubiquitous PPIases (EC 5.2.1.8), which together with FK560 binding proteins (FKBP) and parvulins belong to a superfamily of immunophilins. These three classes of proteins are easily distinguishable by their selective interactions with immunosuppressive drugs. Cyclophilins are targets for cyclosporin A (CsA), parvulins bind juglone (5-hydroxy-1.4-naphthoquinone) and FKBP are inhibited either by FK560 drug or by rapamycin. Despite the lack of structural similarity all these proteins have been shown to act as peptidylprolyl cis-trans isomerases. In all cases binding of the drug inhibits their PPIase activity. Distinct isoforms of cyclophilins have been localized in the cytoplasm, nucleus, mitochondria, chloroplasts and endoplasmic reticulum.
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