Cyclophilins characteristics

Lamos and colleagues reported the modification of cyclophilin A (CypA) by binding immunosuppressive cyclosporin A with a benzophenone-Dj j and a biotin moiety (compound 89, Fig. 11a) [91]. As a proof of principle, they used a 1 1 mixture of this TIP and its nondeuterated isoster for the selective PAL and pulldown of CypA among three other proteins. Subsequent tryptic digestion of the elutes and LC-MS/MS analysis allowed the identification of 11 CypA characteristic peptides, two of which were modified with the probe, as evidenced from the double, 11 Da separated, peaks in the mass spectra. The large 11-Da mass difference allowed easy visual recognition of labeled peptides in the mass spectra, which makes this a powerful method for determination of the modification site after PAL however, application in more complex systems still remains to be done. 

Formerly DUPDl, but does not contain an N-terminal cyclophilin domain, as originally annotated. The mouse ortholog also lacks cyclophilin domain. Thus, the name DUPDl is a misnomer hjumpy lacks any of the typical domains characteristic of the myotubularin family, but it does contain the myotubularin-specif WDR motif within the P loop and does have phosphatidylinositol-... 

Figure 10. Three isoforms of cyclophiliii A associated with human immunodeficiency virus type 1 and proposed model for the localization of each cyclophilin. A. Cellular CyPAs (CyPA6.4o, CyPAe.ss, and CyPAggg) are incorporated into progeny viruses via HIV-1 Gag precursor. Although the mechanisms that permit the redistribution of CyPA on the viral surface are not yet clarified, CyPA itself may have the characteristic of membrane penetrability.

---