ArticleThe Biochemical journal2014
Differential conformational dynamics in the closely homologous FK506-binding domains of FKBP51 and FKBP52.
Article in The Biochemical journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 26 citations in OpenAlex.
- Interplay of p23 with FKBP51 and their chaperone complex in regulating tau aggregation.Nature communications · 2025Article
- Propagation of conformational instability in FK506-binding protein FKBP12.Biochimica et biophysica acta. Proteins and proteomics · 2024Article
- Cryo-EM reveals how Hsp90 and FKBP immunophilins co-regulate the glucocorticoid receptor.Nature structural & molecular biology · 2023Article
- Cryo-EM reveals how Hsp90 and FKBP immunophilins co-regulate the Glucocorticoid Receptor.bioRxiv : the preprint server for biology · 2023Article
- FKBP52 in Neuronal Signaling and Neurodegenerative Diseases: A Microtubule Story.International journal of molecular sciences · 2022Review
- Macrocyclic FKBP51 Ligands Define a Transient Binding Mode with Enhanced Selectivity.Angewandte Chemie (International ed. in English) · 2021Article
- Functional Comparison of Human and Zebra Fish FKBP52 Confirms the Importance of the Proline-Rich Loop for Regulation of Steroid Hormone Receptor Activity.International journal of molecular sciences · 2019Article
- The Many Faces of FKBP51.Biomolecules · 2019Review
- FKBP51 modulates steroid sensitivity and NFκB signalling: A novel anti-inflammatory drug target.European journal of immunology · 2018Article
- Quantifying protein dynamics in the ps-ns time regime by NMR relaxation.Journal of biomolecular NMR · 2016Article
- The role of decidual cells in uterine hemostasis, menstruation, inflammation, adverse pregnancy outcomes and abnormal uterine bleeding.Human reproduction update · 2016Review
- Coupling of Conformational Transitions in the N-terminal Domain of the 51-kDa FK506-binding Protein (FKBP51) Near Its Site of Interaction with the Steroid Receptor Proteins.The Journal of biological chemistry · 2015Article
- Conformational Dynamics in FKBP Domains: Relevance to Molecular Signaling and Drug Design.Current molecular pharmacology · 2015Review
- Statistical allosteric coupling to the active site indole ring flip equilibria in the FK506-binding domain.Biophysical chemistry · 2014Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
As co-chaperones of Hsp90 (heat-shock protein 90), FKBP51 (FK506-binding protein of 51 kDa) and FKBP52 (FK506-binding protein of 52 kDa) act as antagonists in regulating the hormone affinity and nuclear transport of steroid receptor complexes. Exchange of Leu119 in FKBP51 for Pro119 in FKBP52 has been shown to largely reverse the steroid receptor activities of FKBP51 and FKBP52. To examine whether differences in conformational dynamics/plasticity might correlate with changes in the reported receptor activities, 15N-NMR relaxation measurements were carried out on the N-terminal FKBP domains of FKBP51 and FKBP52 as well as their residue-swapped variants. Both proteins exhibit a similar pattern of motion in the picosecond-nanosecond timeframe as well as a small degree of 15N line-broadening, indicative of motion in the microsecond-millisecond timeframe, in the β3a strand of the central sheet. Only the FKBP51 domain exhibits much larger line-broadening in the adjacent β3 bulge (40's loop of FKBP12) and throughout the long β4-β5 loop (80's loop of FKBP12). The L119P mutation at the tip of the β4-β5 loop completely suppressed the line-broadening in this loop while partially suppressing the line-broadening in the neighbouring β2 and β3a strands. The complementary P119L and P119L/P124S variants of FKBP52 yielded similar patterns of line-broadening for the β4-β5 loop as that for FKBP51, although only 20% and 60% as intense respectively. However, despite the close structural similarity in the packing interactions between the β4-β5 loop and the β3a strand for FKBP51 and FKBP52, the line-broadening in the β3a strand is unaffected by the P119L or P119L/P124S mutations in FKBP52.
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Registered trials
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