4lsa
Crystal structure of BRI1 sud1 (Gly643Glu) bound to brassinolideCrystal structure of BRI1 sud1 (Gly643Glu) bound to brassinolide
Structural highlights
FunctionBRI1_ARATH Receptor with a dual specificity kinase activity acting on both serine/threonine- and tyrosine-containing substrates. Regulates, in response to brassinosteroid binding, a signaling cascade involved in plant development, including expression of light- and stress-regulated genes, promotion of cell elongation, normal leaf and chloroplast senescence, and flowering. Binds brassinolide, and less effectively castasterone, but not 2,3,22,23-O-tetramethylbrassinolide or ecdysone. May be involved in a feedback regulation of brassinosteroid biosynthesis. Phosphorylates BRI1-associated receptor kinase 1 (BAK1), Transthyretin-Like protein (TTL) and SERK1 on 'Ser-299' and 'Thr-462' in vitro. May have a guanylyl cyclase activity.[1] [2] [3] [4] [5] [6] Publication Abstract from PubMedBrassinosteroids, 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. Molecular mechanism for plant steroid receptor activation by somatic embryogenesis co-receptor kinases.,Santiago J, Henzler C, Hothorn M Science. 2013 Aug 23;341(6148):889-92. doi: 10.1126/science.1242468. Epub 2013, Aug 8. PMID:23929946[7] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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