Structure and Function of Cyclophilins
Komitet Biotechnologii PAN ; Instytut Chemii Bioorganicznej PAN
Cyclophilins (CyPs) constitute a large class of highly conserved, ubiquitousPPlases (EC 5.2.1.8) that together with FK560 binding proteins (FKBP) and parvulinsbelong to a superfamily of immunophilins. These three classes of proteins areeasily distinguishable by their selective interactions with immunosuppressivedrugs. Cyclophilins are targets for cyclosporin A (CsA), parvulins bind juglone(5-hydroxy-l.4-naphthoquinone) and FKBP, they are inhibited either by FK560drug or by rapamycin. Despite the lack of structural similarity, all these proteinshave been shown to act as peptidylprolyl cis-trans isomerases. In all cases, binding of the drug inhibits their PPIase activity. Distinct isoforms of cyclophilinshave been localized in the cytoplasm, nucleus, mitochondria, chloroplasts andendoplasmic reticulum.
Biotechnologia, vol.58, 3 (2002)-.
0860-7796 ; oai:rcin.org.pl:137917 ; IChB B-54
Biblioteka Instytutu Chemii Bioorganicznej PAN
Licencja Creative Commons Uznanie autorstwa-Na tych samych warunkach 4.0
Instytut Chemii Bioorganicznej Polskiej Akademii Nauk
Instytut Chemii Bioorganicznej Polskiej Akademii Nauk
Oct 2, 2020
Sep 4, 2020
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https://rcin.org.pl./publication/173026
Edition name | Date |
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Struktura i funkcja cyklofillin | Oct 2, 2020 |
Borkowska, Bożenna
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Lipiński, Daniel Szalata, Marlena Kalak, Robert Pławski, Andrzej Nuc, Katarzyna Kala, Marta Juzwa, Wojciech Słomska, Karolina Gronek, Piotr Jura, Jacek Jura, Jolanta Smorąg, Zdzisław Pieńkowski, Marek Słomski, Ryszard
Nowak, Jacek K.
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