Subtitle:

Structure and Function of Cyclophilins

Publisher:

Committee on Biotechnology PAS ; Institute of Bioorganic Chemistry PAS

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:

58

Issue:

3

Start page:

135

End page:

152

Detailed Resource Type:

Article

Format:

application/pdf

Resource Identifier:

0860-7796 ; oai:rcin.org.pl:137917 ; IChB B-54

Source:

Library of Institute of Bioorganic Chemistry PAS

Language:

pol

Language of abstract:

eng

Temporal coverage:

1988-2010

Rights:

Creative Commons Attribution BY-SA 4.0 license

Terms of use:

Copyright-protected material. [CC BY-SA 4.0] May be used within the scope specified in Creative Commons Attribution BY-SA 4.0 license, full text available at:

Digitizing institution:

Institute of Bioorganic Chemistry of the Polish Academy of Science

Original in:

Institute of Bioorganic Chemistry of the Polish Academy of Science

Projects co-financed by:

Operational Program Digital Poland, 2014-2020, Measure 2.3: Digital accessibility and usefulness of public sector information; funds from the European Regional Development Fund and national co-financing from the state budget.

Access:

Open