Trehalose Induces Functional Conformation in Glucocorticoid Receptor Activation Domain
Author Information
Author(s): Khan Shagufta H., Arnott John A., Kumar Raj
Primary Institution: The Commonwealth Medical College
Hypothesis
Can trehalose promote functionally ordered conformation in the glucocorticoid receptor's activation function domain?
Conclusion
Trehalose induces an ordered conformation in the glucocorticoid receptor's activation domain, enhancing its interaction with coregulatory proteins.
Supporting Evidence
- Trehalose induces a compact structure in the glucocorticoid receptor's activation domain.
- Trehalose-induced conformational transition in the activation domain is cooperative in nature.
- Presence of trehalose protects the activation domain from proteolysis.
- Trehalose enhances the binding of the glucocorticoid receptor to its response element DNA.
- Trehalose-induced folding facilitates interaction with the coactivator SRC-1.
Takeaway
Trehalose helps a part of a protein called the glucocorticoid receptor fold into a shape that works better with other proteins.
Methodology
The study used circular dichroism spectroscopy, limited proteolytic digestion, electro-mobility shifting assays, and immunoprecipitation to analyze the effects of trehalose on the glucocorticoid receptor's activation domain.
Limitations
The concentrations of trehalose used in vitro may not reflect typical intracellular conditions.
Digital Object Identifier (DOI)
Want to read the original?
Access the complete publication on the publisher's website