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Structure and Function of Cyclophilins
Subtitle:Structure and Function of Cyclophilins
Creator:Nuc, Katarzyna ; Słomski, Ryszard
Publisher:Committee on Biotechnology PAS ; Institute of Bioorganic Chemistry PAS
Date issued/created: Subject and Keywords: Abstract: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.
Relation:Biotechnologia, vol.58, 3 (2002)-.
Volume: Issue: Start page: End page: Resource type: Detailed Resource Type: Format: Resource Identifier: Source:Library of Institute of Bioorganic Chemistry PAS
Language: Language of abstract: Temporal coverage: Rights:Creative Commons Attribution BY-SA 4.0 license
Terms of use: Digitizing institution:Institute of Bioorganic Chemistry of the Polish Academy of Science
Original in:Institute of Bioorganic Chemistry of the Polish Academy of Science
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