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We propose a model in which heterodimerisa-tion of the BRI1 and SERK ectodomains brings their cytoplasmic kinase domains in a catalytically competent arrangement, an interaction that can be modulated by the BRI1 inhibitor protein BKI1. We identify a protein interaction surface on the C-terminal lobe of the kinase and demonstrate that the isolated BRI1, SERK2 and SERK3 cytoplasmic segments form homodi-mers in solution and have a weak tendency to heteromerise. The location of known genetic missense alleles provide detailed insight into the BRI1 kinase mechanism, while our analyses are inconsistent with a previously reported guanylate cyclase activity. Phosphorylation of Thr, Ser and Ser causes formation of a catalytically competent activation loop. Here we report crystal structures of the BRI1 kinase domain in its activated form and in complex with nucleotides. Saravanathamizhan, Veerappan Ramamurthi. This way, the user would be able to educate himself in professional photography and will learn step y step. Offers to the user, along with inspirational content from established photographers.
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