STRUCTURE OF FKBP59-I, THE N-TERMINAL DOMAIN OF A 59 KDA FK506-BINDING PROTEIN, NMR, MINIMIZED AVERAGE STRUCTURESTRUCTURE OF FKBP59-I, THE N-TERMINAL DOMAIN OF A 59 KDA FK506-BINDING PROTEIN, NMR, MINIMIZED AVERAGE STRUCTURE

Structural highlights

1rot is a 1 chain structure with sequence from Oryctolagus cuniculus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FKBP4_RABIT Immunophilin protein with PPIase and co-chaperone activities. Component of unligated steroid receptors heterocomplexes thought interaction with heat-shock protein 90 (HSP90) (By similarity). May play a role in the intracellular trafficking of heterooligomeric forms of steroid hormone receptors between cytoplasm and nuclear compartments. The isomerase activity controls neuronal growth cones via regulation of TRPC1 channel opening. May have a protective role against oxidative stress in mitochondria (By similarity). Acts also as a regulator of microtubule dynamics by inhibiting MAPT/TAU ability to promote microtubule assembly.[1]

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

  1. Pirkl F, Fischer E, Modrow S, Buchner J. Localization of the chaperone domain of FKBP52. J Biol Chem. 2001 Oct 5;276(40):37034-41. Epub 2001 Jul 25. PMID:11473108 doi:http://dx.doi.org/10.1074/jbc.M102595200
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