Structure and function of cyclophilins
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Cyclophilins (CyPs) constitute a large class of highly conserved, ubiquitous PPIases (EC 220.127.116.11), 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.
Publication order reference
K.Nuc, Katedra Biochemii i Biotechnologii, Akademia Rolnicza im. Augusta Cieszkowskiego, ul. Wolynska 33, 60-637 Poznan, Poland