Structural Basis for Assembly and Function of a Heterodimeric Plant Immune Receptor

@article{Williams2014StructuralBF,
  title={Structural Basis for Assembly and Function of a Heterodimeric Plant Immune Receptor},
  author={Simon J Williams and Kee Hoon Sohn and Li Wan and Maud Bernoux and Panagiotis F Sarris and C{\'e}cile Segonzac and Thomas Ve and Yan Ma and Simon B Saucet and Daniel Jesper Ericsson and Lachlan W. Casey and Thierry G. A. Lonhienne and Donald J Winzor and Xiao-xiao Zhang and Anne Coerdt and Jane E Parker and Peter N Dodds and Bostjan Kobe and Jonathan D. G. Jones},
  journal={Science},
  year={2014},
  volume={344},
  pages={299-303}
}
Cytoplasmic plant immune receptors recognize specific pathogen effector proteins and initiate effector-triggered immunity. In Arabidopsis, the immune receptors RPS4 and RRS1 are both required to activate defense to three different pathogens. We show that RPS4 and RRS1 physically associate. Crystal structures of the N-terminal Toll–interleukin-1 receptor/resistance (TIR) domains of RPS4 and RRS1, individually and as a heterodimeric complex (respectively at 2.05, 1.75, and 2.65 angstrom… CONTINUE READING
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