Structural basis of steroid hormone perception by the receptor kinase BRI1

Michael Hothorn, Youssef Belkhadir, Marlene Dreux, Tsegaye Dabi, Joseph. P. Noel, Ian A. Wilson and Joanne Chory ()
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Michael Hothorn: Plant Biology Laboratory, The Salk Institute for Biological Studies, 10010 North Torrey Pines Road, La Jolla, California 92037, USA
Youssef Belkhadir: Plant Biology Laboratory, The Salk Institute for Biological Studies, 10010 North Torrey Pines Road, La Jolla, California 92037, USA
Marlene Dreux: The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, USA
Tsegaye Dabi: Plant Biology Laboratory, The Salk Institute for Biological Studies, 10010 North Torrey Pines Road, La Jolla, California 92037, USA
Joseph. P. Noel: Howard Hughes Medical Institute, The Salk Institute for Biological Studies, 10010 North Torrey Pines Road, La Jolla, California 92037, USA
Ian A. Wilson: The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, USA
Joanne Chory: Plant Biology Laboratory, The Salk Institute for Biological Studies, 10010 North Torrey Pines Road, La Jolla, California 92037, USA

Nature, 2011, vol. 474, issue 7352, 467-471

Abstract: Abstract 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.

Date: 2011
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DOI: 10.1038/nature10153

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