Crystal structure of the leucine-rich repeat ectodomain of the plant immune receptor kinase SOBIR1

Plant-unique membrane receptor kinases with leucine-rich repeat (LRR) extracellular domains are key regulators of development and immune responses. Here, the 1.55   Å resolution crystal structure of the immune receptor kinase SOBIR1 from Arabidopsis is presented. The ectodomain structure reveals the presence of five LRRs sandwiched between noncanonical capping domains. The disulfide-bond-stabilized N-terminal cap harbours an unusual β -hairpin structure. The C-terminal cap features a highly positively charged linear motif which was found to be largely disordered in this structure. Size-exclusion chromatography and right-angle light-scattering experiments suggest that SOBIR1 is a monomer in solution. The protruding β -hairpin, a set of highly conserved basic residues at the inner surface of the SOBIR LRR domain and the presence of a genetic missense allele in LRR2 together suggest that the SOBIR1 ectodomain may mediate protein – protein interaction in plant immune signalling.
Source: Acta Crystallographica Section D - Category: Biochemistry Authors: Tags: leucine-rich repeat ectodomain receptor kinase plant immune signalling Arabidopsis cell signalling membrane receptor research papers Source Type: research