3RJ0
Plant steroid receptor BRI1 ectodomain in complex with brassinolide
Summary for 3RJ0
| Entry DOI | 10.2210/pdb3rj0/pdb |
| Related | 3RIZ |
| Descriptor | Protein BRASSINOSTEROID INSENSITIVE 1, alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total) |
| Functional Keywords | superhelix, island domain, leucine-rich repeat, steroid receptor, hormone receptor, receptor kinase, brassinosteroid binding, n-glycosylation, plasma membrane and endosomes, signaling protein |
| Biological source | Arabidopsis thaliana (mouse-ear cress) |
| Cellular location | Cell membrane; Single-pass type I membrane protein: O22476 |
| Total number of polymer chains | 1 |
| Total formula weight | 86884.74 |
| Authors | Hothorn, M. (deposition date: 2011-04-14, release date: 2011-06-22, Last modification date: 2020-07-29) |
| Primary citation | Hothorn, M.,Belkhadir, Y.,Dreux, M.,Dabi, T.,Noel, J.P.,Wilson, I.A.,Chory, J. Structural basis of steroid hormone perception by the receptor kinase BRI1. Nature, 474:467-471, 2011 Cited by PubMed 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. PubMed: 21666665DOI: 10.1038/nature10153 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.541 Å) |
Structure validation
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