4lsc | pdb_00004lsc

Isolated SERK1 co-receptor ectodomain at high resolution

spinqualitylabelsall models 4lsc, resolution 1.53Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4lsc is a 1 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BMA, NAG, FUC Related: 3riz, 3rj0, 4lsa, 4lsx Gene: At1g71830, F14O23.21, F14O23_24, SERK1 (Arabidopsis thaliana) Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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