3RJ0

Plant steroid receptor BRI1 ectodomain in complex with brassinolide

3RJ0 の概要

• エントリーDOI: 10.2210/pdb3rj0/pdb
• 関連するPDBエントリー: 3RIZ
• 分子名称: 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)
• 機能のキーワード: superhelix, island domain, leucine-rich repeat, steroid receptor, hormone receptor, receptor kinase, brassinosteroid binding, n-glycosylation, plasma membrane and endosomes, signaling protein
• 由来する生物種: Arabidopsis thaliana (mouse-ear cress)
• 細胞内の位置: Cell membrane; Single-pass type I membrane protein: O22476
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 86884.74

構造登録者

Hothorn, M. (登録日: 2011-04-14, 公開日: 2011-06-22, 最終更新日: 2020-07-29)

主引用文献

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

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: 21666665
DOI: 10.1038/nature10153

実験手法

X-RAY DIFFRACTION (2.541 Å)