Editors' ChoiceStructural Biology

Universal Immune Function

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Science Signaling  22 Apr 2014:
Vol. 7, Issue 322, pp. ec110
DOI: 10.1126/scisignal.2005398

Certain pathogen effectors are detected in plants by cytoplasmic receptors. First solving the crystal structures of Arabidopsis receptors, Williams et al. (see the Perspective by Nishimura and Dangl) discovered that in the resting state, the structures form a heterodimer that readies the complex for effector binding and keeps the signaling domains from firing too early. Once the pathogen effector binds, the structure of the complex shifts such that the signaling domains can form a homodimer to initiate downstream signaling. Similarities between these plant-pathogen receptors and Toll-like receptors in animals suggest that the molecular mechanisms may translate broadly.

S. J. Williams, K. H. Sohn, L. Wan, M. Bernoux, P. F. Sarris, C. Segonzac, T. Ve, Y. Ma, S. B. Saucet, D. J. Ericsson, L. W. Casey, T. Lonhienne, D. J. Winzor, X. Zhang, A. Coerdt, J. E. Parker, P. N. Dodds, B. Kobe, J. D. G. Jones, Structural basis for assembly and function of a heterodimeric plant immune receptor. Science 344, 299–303 (2014). [Abstract] [Full Text]

M. T. Nishimura, J. L. Dangl, Paired plant immune receptors. Science 344, 267–268 (2014).[Abstract] [Full Text]

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