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Gene Review:

CyP22 - peptidyl-prolyl cis-trans isomerase

Plasmodium falciparum 3D7

Gavigan, C.S. et al., Yarovinsky, F. et al.

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Disease relevance of PF11_0164

In contrast, four mutations in C-18 specifically designed to abolish the peptidyl-prolyl cis-trans-isomerase activity of the protein failed to inactivate its CCR5 binding and HIV inhibitory activities [1].

High impact information on PF11_0164

The peptidyl-prolyl cis-trans isomerase activity of recombinant PfCyP-19B had the same profile of susceptibility to cyclosporin derivatives as the bulk isomerase activity of crude P. falciparum extracts [2].

References

Structural determinants of the anti-HIV activity of a CCR5 antagonist derived from Toxoplasma gondii. Yarovinsky, F., Andersen, J.F., King, L.R., Caspar, P., Aliberti, J., Golding, H., Sher, A. J. Biol. Chem. (2004) [Pubmed]
Cyclosporin-binding proteins of Plasmodium falciparum. Gavigan, C.S., Kiely, S.P., Hirtzlin, J., Bell, A. Int. J. Parasitol. (2003) [Pubmed]

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