Crystal Structures of the Free and Ligand-Bound FK1–FK2 Domain Segment of FKBP52 Reveal a Flexible Inter-Domain Hinge
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Structural Biology
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1. Cryo-EM reveals how Hsp90 and FKBP immunophilins co-regulate the glucocorticoid receptor;Nature Structural & Molecular Biology;2023-11-09
2. Large-scale, in-cell photocrosslinking at single-residue resolution reveals the molecular basis for glucocorticoid receptor regulation by immunophilins;Nature Structural & Molecular Biology;2023-11-09
3. Transient conformations in the unliganded FK506 binding domain of FKBP51 correspond to two distinct inhibitor-bound states;Journal of Biological Chemistry;2023-09
4. Structure and function of the TPR‐domain immunophilins FKBP51 and FKBP52 in normal physiology and disease;Journal of Cellular Biochemistry;2023-04-23
5. Large-scale in-cell photocrosslinking at single residue resolution reveals the molecular basis for glucocorticoid receptor regulation by immunophilins;2023-01-19
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