Structure of the <i>Arabidopsis </i>receptor kinase SRF6 ectodomain determined from crystals obtained using the LRR crystallization screen

Article Article scientifique Article Structure of the <i>Arabidopsis </i>receptor kinase SRF6 ectodomain determined from crystals obtained using the LRR crystallization screen eng 2026-06-12 2026-07-01 author Caregnato Alberto Francesco 0000-0003-2687-3662 Structural Plant Biology Laboratory, Department of Plant Science, University of Geneva, 1211 Geneva, Switzerland. 969750 Département des sciences végétales (BIVEG) author Hohmann Ulrich 0000-0003-2124-1439 Structural Plant Biology Laboratory, Department of Plant Science, University of Geneva, 1211 Geneva, Switzerland. 823897 author Hothorn Michael 0000-0002-3597-5698 Structural Plant Biology Laboratory, Department of Plant Science, University of Geneva, 1211 Geneva, Switzerland. 826130 Département des sciences végétales (BIVEG) 10.1107/S2059798326005498 42283205 2059-7983 Plant-specific membrane receptor kinases with structurally diverse extracellular domains regulate key processes in plant growth, development, immunity and symbiosis. Structural studies of these glycoproteins are often hampered by the limited quantities in which they can be obtained. Here, we describe the leucine-rich repeat (LRR) crystallization screen, which has enabled the successful crystallization and structure determination of multiple receptor kinase ectodomains, including ligand- and co-receptor-bound complexes. As an example, we report the 1.5 Å resolution crystal structure of the LRR domain of STRUBBELIG-RECEPTOR FAMILY 6 (SRF6) from Arabidopsis thaliana. The SRF6 ectodomain contains seven LRRs and a disulfide-bond-stabilized N-terminal capping domain but lacks the canonical C-terminal cap and the N-glycosylation pattern typically found in other family members. Previously reported protein-protein interactions between the SRF6 and SRF7 ectodomains and the receptor kinases BRI1, BRL1, BRL3, SERK3 and BIR1-BIR3 could not be confirmed by quantitative isothermal titration calorimetry and grating-coupled interferometry assays, suggesting that these structurally conserved LRR receptor kinases may have signalling functions outside the brassinosteroid pathway. Arabidopsis thaliana Crystallization screens Ectodomains Leucine-rich repeats Membrane receptors Plant development Dewey 580 Swiss National Science Foundation Structural and functional investigation of plant membrane receptor kinases and their cytoplasmic signaling cascades 205201 CH 45 Département des sciences végétales 163 false 830 Groupe Hothorn Acta crystallographica. Section D, Structural biology 82 7 9dc59d67-a850-4736-89b0-b1fe5dcbc9b4 Article (Published version) Public jb5072.pdf 11450753 application/pdf CC BY-4.0 d8a5e4bf254596013e6aded92af38ccada2160b11393a11718fc642ab3b8604f openAccess Faculté des sciences / Section de biologie / Département des sciences végétales

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Structure of the Arabidopsis receptor kinase SRF6 ectodomain determined from crystals obtained using the LRR crystallization screen	Acta crystallographica. Section D, Structural biology			2026	3	4

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Caregnato, Alberto Francesco