Structural highlights
Function
PPID_BOVIN PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Proposed to act as a co-chaperone in HSP90 complexes such as in unligated steroid receptors heterocomplexes. Different co-chaperones seem to compete for association with HSP90 thus establishing distinct HSP90-co-chaperone-receptor complexes with the potential to exert tissue-specific receptor activity control. May have a preference for estrogen receptor complexes and is not found in glucocorticoid receptor complexes. May be involved in cytoplasmic dynein-dependent movement of the receptor from the cytoplasm to the nucleus. May regulate MYB by inhibiting its DNA-binding activity. Involved in regulation of AHR signaling by promoting the formation of the AHR:ARNT dimer; the function is independent of HSP90 but requires the chaperone activity. Involved in regulation of UV radiation-induced apoptosis.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
See Also
References
- ↑ Kieffer LJ, Thalhammer T, Handschumacher RE. Isolation and characterization of a 40-kDa cyclophilin-related protein. J Biol Chem. 1992 Mar 15;267(8):5503-7. PMID:1544925
- ↑ Mok D, Allan RK, Carrello A, Wangoo K, Walkinshaw MD, Ratajczak T. The chaperone function of cyclophilin 40 maps to a cleft between the prolyl isomerase and tetratricopeptide repeat domains. FEBS Lett. 2006 May 15;580(11):2761-8. Epub 2006 Apr 24. PMID:16650407 doi:http://dx.doi.org/10.1016/j.febslet.2006.04.039
