Immunophilins: structure—function relationship and possible role in microbial pathogenicity

@article{Hacker1993ImmunophilinsSR,
  title={Immunophilins: structure—function relationship and possible role in microbial pathogenicity},
  author={J{\"o}rg H Hacker and Gunter Fischer},
  journal={Molecular Microbiology},
  year={1993},
  volume={10}
}
Immunophilins are housekeeping proteins present in a wide variety of organisms. Members of two protein superfamilies, cyclophilins (Cyps) and FK506‐binding proteins (FKBPs) belong to this class of immunophilins. Despite the fact that the amino acid sequences of Cyp and FKBPs do not exhibit noticeable homology to each other, proteins of both classes are able to ligate immunosuppressive peptide derivatives. Cyps form complexes with the cyclic undecapeptide cyclosporin A and FKBPs are able to bind… 

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    Proceedings of the National Academy of Sciences of the United States of America
  • 1992
Using the polymerase chain reaction, a homolog of an FK506-binding protein from Neisseria meningitidis is cloned and sequenced and expressed the gene product as a fusion protein with maltose-bindingprotein, which had rotamase activity comparable to that of human Fk506- binding protein.

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