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Journal
2002 | 3 | 135-152
Article title

Structure and function of cyclophilins

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Languages of publication
PL
Abstracts
EN
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.
Publisher

Journal
Year
Issue
3
Pages
135-152
Physical description
Contributors
author
author
References
Document Type
REVIEW
Publication order reference
K.Nuc, Katedra Biochemii i Biotechnologii, Akademia Rolnicza im. Augusta Cieszkowskiego, ul. Wolynska 33, 60-637 Poznan, Poland
Identifiers
YADDA identifier
bwmeta1.element.element-from-psjc-efb40f10-6328-31a9-a08a-e9453c4e889a
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