Disease relevance of CPR6

• The cDNA was engineered for expression in Escherichia coli, and the resulting recombinant protein, like mammalian Cyps, exhibited a peptidyl-prolyl cis-trans isomerase (PPIase) activity which was sensitive to inhibition by cyclosporin A in vitro [1].

High impact information on CPR6

• Sti1 and Cpr6 both bind with sub-micromolar affinity, with Sti1 binding accompanied by a large conformational change [2].
• Transport kinetic studies indicated that nuclear export of Zpr1p was defective in cpr1Delta cells, and rescue of this defect correlated with PPIase activity [3].
• There are two cyclophilin 40 homologs in the yeast Saccharomyces cerevisiae, encoded by the CPR6 and CPR7 genes [4].
• Affinity isolation of histidine-tagged Sba1p (Sba1(His6)) after expression in yeast led to coisolation of Hsp90 and the cyclophilin homolog Cpr6 [5].
• Pin1/Ess1p is a highly conserved WW domain-containing peptidyl-prolyl isomerase (PPIase); its WW domain binds specifically to phospho-Ser/Thr-Pro sequences and its catalytic domain isomerizes phospho-Ser/Thr-Pro bonds [6].

Biological context of CPR6

• Neither CPR6 nor CPR7 is essential but deletion of CPR7 results in a significant impairment of the rate of cell division [7].
• RESULTS: PPIase numbers within these fungal repertoires appears associated with genome size and orthology between repertoires was found to be low [8].

Associations of CPR6 with chemical compounds

• Characterization of NcCyP41 reveals that it is a heat shock protein, which is active as a cyclosporin A-sensitive PPIase [9].

References