3KZ7

Diversified targets of FKBP25 and its complex with rapamycin.

(2014) Int J Biol Macromol 69: 344-352

• PubMed: 24879919 Search on PubMed
• DOI: https://doi.org/10.1016/j.ijbiomac.2014.05.060
• Primary Citation of Related Structures:  
  3KZ7


• PubMed Abstract: 
  

  FKBP25 is a member of the super-family of peptidylprolyl cis/trans isomerases, which is a high affinity binder for the immunosuppressive antibiotic rapamycin (Rpm). FKBP25 isolated from natural sources, its recombinant murine homologue (mFKBP25) and their complexes with rapamycin bind to diverse DNAs, RNAs and heparin affinity beads. The recombinant mFKBP25/rapamycin complex binds to several proteins including the calcineurin-A/calcineurin-B/calmodulin complex and to elongation factor 1β. We solved the X-ray structure of the C-terminal domain of mFKBP25 bound to rapamycin that has a higher resolution than of its human counterpart, and which clearly illustrates that the positively charged 40s loop is an epitope of the FK506-like binding domain (FKBD) for interactions with various biopolymers.

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Organizational Affiliation: 

Commissariat à l'Energie Atomique, Direction des Sciences du Vivant, Institut de Biologie et de Technologies de Saclay, Service d'Ingénierie Moléculaire des Protéines, Gif sur Yvette F-91191, France. Electronic address: galat@dsvidf.cea.fr.