The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Structural basis of steroid hormone perception by the receptor kinase BRI1
Open accessAbstract
Polyhydroxylated steroids are regulators of body shape and size in higher organisms. In metazoans, intracellular receptors recognize these molecules. Plants, however, perceive steroids at membranes, using the membrane-integral receptor kinase BRASSINOSTEROID INSENSITIVE 1 (BRI1). Here we report the structure of the Arabidopsis thaliana BRI1 ligand-binding domain, determined by X-ray diffraction at 2.5 Å resolution. We find a superhelix of 25 twisted leucine-rich repeats (LRRs), an architecture that is strikingly different from the assembly of LRRs in animal Toll-like receptors. A 70-amino-acid island domain between LRRs 21 and 22 folds back into the interior of the superhelix to create a surface pocket for binding the plant hormone brassinolide. Known loss- and gain-of-function mutations map closely to the hormone-binding site. We propose that steroid binding to BRI1 generates a docking platform for a co-receptor that is required for receptor activation. Our findings provide insight into the activation mechanism of this highly expanded family of plant receptors that have essential roles in hormone, developmental and innate immunity signalling.
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Coot : model-building tools for molecular graphics
Emsley, P., & Cowtan, K. (2004) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444904019158 · Cited by 30,571
The nuclear receptor superfamily: the second decade
Mangelsdorf, D. J., Thummel, C., Beato, M., Herrlich, P., Schütz, G., Umesono, K., Blumberg, B., Kastner, P., Mark, M., Chambon, P., et al. (1995) · Cell · doi:10.1016/0092-8674(95)90199-x · Cited by 6,964
Terwilliger, T. C., Grosse-Kunstleve, R. W., Afonine, P. V., Moriarty, N. W., Zwart, P. H., Hung, L.-W., Read, R. J., & Adams, P. D. (2008) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s090744490705024x · Cited by 1,462
BRI1/BAK1, a Receptor Kinase Pair Mediating Brassinosteroid Signaling
Nam, K. H., & Li, J. (2002) · Cell · doi:10.1016/s0092-8674(02)00814-0 · Cited by 1,217
Schubert, W.-D., Urbanke, C., Ziehm, T., Beier, V., Machner, M. P., Domann, E., Wehland, J., Chakraborty, T., & Heinz, D. W. (2002) · Cell · doi:10.1016/s0092-8674(02)01136-4 · Cited by 302
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Brassinosteroid Signaling Network and Regulation of Photomorphogenesis
Wang, Z.-Y., Bai, M.-Y., Oh, E., & Zhu, J.-Y. (2012) · Annual Review of Genetics · doi:10.1146/annurev-genet-102209-163450 · Cited by 490
Santiago, J., Henzler, C., & Hothorn, M. (2013) · Science · doi:10.1126/science.1242468 · Cited by 357
Self-citationStressed Out About Hormones: How Plants Orchestrate Immunity
Bürger, M., & Chory, J. (2019) · Cell Host & Microbe · doi:10.1016/j.chom.2019.07.006 · Cited by 312
Self-citationStructure reveals that BAK1 as a co-receptor recognizes the BRI1-bound brassinolide
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Metadata
- Authors
- Hothorn, M., Belkhadir, Y., Dreux, M., Dabi, T., Noel, J. P., Wilson, I. A., & Chory, J.
- Venue
- Nature
- Published
- 2011-06
- Volume
- 474
- Issue
- 7352
- Pages
- 467-471
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2062801286
- Cited by
- 420
- References
- 5
- FWCI
- 40.32
- Type
- journal article
- Language
- en
- Open access
- green
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- Hothorn, M., Belkhadir, Y., Dreux, M., Dabi, T., Noel, J. P., Wilson, I. A., & Chory, J. (2011). Structural basis of steroid hormone perception by the receptor kinase BRI1. Nature. https://doi.org/10.1038/nature10153
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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