Cryo-EM structure of the GR-Hsp90-FKBP51 complex

Cryo-EM reveals how Hsp90 and FKBP immunophilins co-regulate the glucocorticoid receptor

Complex of the Glucocorticoid Receptor ligand binding domain, Hsp90 alpha dimer, and the co-chaperone FKBP51

Peptidyl-prolyl cis-trans isomerase FKBP5

Heat shock 86 kDa,HSP 86,HSP86,Lipopolysaccharide-associated protein 2,LAP-2,LPS-associated protein 2,Renal carcinoma antigen NY-REN-38

GR,Nuclear receptor subfamily 3 group C member 1

PPIase FKBP5,51 kDa FK506-binding protein,51 kDa FKBP,FKBP-51,54 kDa progesterone receptor-associated immunophilin,Androgen-regulated protein 6,FF1 antigen,FK506-binding protein 5,FKBP-5,FKBP54,p54,HSP90-binding immunophilin,Rotamase

National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)

chaperone, steroid hormone receptor, ligand binding, ATP binding, protein folding