Structure， Subcellular Localization and Biological Function of Cyclophilin

Abstract: Cyclophilin (CyP) belongs to a family of highly conserved and multifunctional protein that is found in both prokaryotes and eukaryotes. CyP possesses peptidyl-prolyl cis-trans isomerase (PPIase) activity which can catalyze the interconvertion of the cis and trans isomers of the peptidyl-prolyl bonds in peptide and affect the process of protein folding and assembling. In addition， CyP can work as molecule chaperones and plays roles in signalling pathways regulation under stress condition and RNA splicing. Since the initial discovery of CyP that is the intracellular target of the immunosuppressant drug cyclosporin A (CsA)， about 130 CyPs isoforms have been identified in different organisms from bacteria to mammal. All members of CyP family have different molecular weight， distinct location and varying function. This paper describes the research history of CyP and introduces the structure， location， function and the relationship of CyP with CsA.

CSTR: 32200.14.cjcb.2008.03.0003