4LSA

Crystal structure of BRI1 sud1 (Gly643Glu) bound to brassinolide

4LSA の概要

• エントリーDOI: 10.2210/pdb4lsa/pdb
• 関連するPDBエントリー: 3RIZ 3RJ0 4LSC 4LSX
• 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: lrr-domain, membrane receptor, brassinosteroid binding, n-glycosylation, protein binding, steroid binding 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: 87338.15

構造登録者

Santiago, J.,Henzler, C.,Hothorn, M. (登録日: 2013-07-22, 公開日: 2013-09-04, 最終更新日: 2024-11-06)

主引用文献

Santiago, J.,Henzler, C.,Hothorn, M.
Molecular mechanism for plant steroid receptor activation by somatic embryogenesis co-receptor kinases.
Science, 341:889-892, 2013

PubMed Abstract: Brassinosteroids, which control plant growth and development, are sensed by the leucine-rich repeat (LRR) domain of the membrane receptor kinase BRASSINOSTEROID INSENSITIVE 1 (BRI1), but it is unknown how steroid binding at the cell surface activates the cytoplasmic kinase domain of the receptor. A family of somatic embryogenesis receptor kinases (SERKs) has been genetically implicated in mediating early brassinosteroid signaling events. We found a direct and steroid-dependent interaction between the BRI1 and SERK1 LRR domains by analysis of their complex crystal structure at 3.3 angstrom resolution. We show that the SERK1 LRR domain is involved in steroid sensing and, through receptor-co-receptor heteromerization, in the activation of the BRI1 signaling pathway. Our work reveals how known missense mutations in BRI1 and in SERKs modulate brassinosteroid signaling and the targeting mechanism of BRI1 receptor antagonists.

PubMed: 23929946
DOI: 10.1126/science.1242468

実験手法

X-RAY DIFFRACTION (2.5 Å)