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The Three-dimensional Structures of Antagonistic and Agonistic Forms of the Glucocorticoid Receptor Ligand-binding Domain
Open accessAbstract
Here we describe the three-dimensional crystal structures of human glucocorticoid receptor ligand-binding domain (GR-LBD) in complex with the antagonist RU-486 at 2.3 A resolution and with the agonist dexamethasone ligand together with a coactivator peptide at 2.8 A. The RU-486 structure was solved in several different crystal forms, two with helix 12 intact (GR1 and GR3) and one with a protease-digested C terminus (GR2). In GR1, part of helix 12 is in a position that covers the co-activator pocket, whereas in the GR3, domain swapping is seen between the crystallographically identical subunits in the GR dimer. An arm consisting of the end of helix 11 and beyond stretches out from one molecule, and helix 12 binds to the other LBD, partly blocking the coactivator pocket of that molecule. This type of GR-LBD dimer has not been described before but might be an artifact from crystallization. Furthermore, the subunits of the GR3 dimers are covalently connected via a disulfide bond between the Cys-736 residues in the two molecules. All three RU-486 GR-LBD structures show that GR has a very flexible region between the end of helix 11 and the end of helix 12.
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[20] Processing of X-ray diffraction data collected in oscillation mode
Otwinowski, Z., & Minor, W. (1997) · Methods in Enzymology · doi:10.1016/s0076-6879(97)76066-x · Cited by 33,475
Deciphering the Phosphorylation “Code” of the Glucocorticoid Receptor in Vivo
Wang, Z., Frederick, J., & Garabedian, M. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m110530200 · Cited by 321
GLUCOCORTICOID AND MINERALOCORTICOID RECEPTORS: Biology and Clinical Relevance
Funder, M. (1997) · Annual Review of Medicine · doi:10.1146/annurev.med.48.1.231 · Cited by 320
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Glucocorticoid receptor control of transcription: precision and plasticity via allostery
Weikum, E. R., Knuesel, M. T., Ortlund, E. A., & Yamamoto, K. R. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.152 · Cited by 533
Structural Overview of the Nuclear Receptor Superfamily: Insights into Physiology and Therapeutics
Huang, P., Chandra, V., & Rastinejad, F. (2010) · Annual Review of Physiology · doi:10.1146/annurev-physiol-021909-135917 · Cited by 533
The human glucocorticoid receptor: molecular basis of biologic function
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Fluorine in Medicinal Chemistry
Swallow, S. (2015) · Progress in Medicinal Chemistry · doi:10.1016/bs.pmch.2014.11.001 · Cited by 280
Metadata
- Authors
- Kauppi, B., Jakob, C., Färnegårdh, M., Yang, J., Ahola, H., Alarcon, M., Calles, K., Engström, O., Harlan, J., Muchmore, S., Ramqvist, A.-K., Thorell, S., Öhman, L., Greer, J., Gustafsson, J.-Å., Carlstedt-Duke, J., & Carlquist, M.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2003-06
- Volume
- 278
- Issue
- 25
- Pages
- 22748-22754
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2139031643
- Cited by
- 336
- References
- 3
- FWCI
- 12.56
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Kauppi, B., Jakob, C., Färnegårdh, M., Yang, J., Ahola, H., Alarcon, M., Calles, K., Engström, O., Harlan, J., Muchmore, S., Ramqvist, A.-K., Thorell, S., Öhman, L., Greer, J., Gustafsson, J.-Å., Carlstedt-Duke, J., & Carlquist, M. (2003). The Three-dimensional Structures of Antagonistic and Agonistic Forms of the Glucocorticoid Receptor Ligand-binding Domain. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m212711200
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
