The N-terminal domain of the tomato immune protein prf contains multiple homotypic and pto kinase interaction sites

Isabel Marie Luise Saur, Brendon Francis Conlan, John Paul Rathjen*

*Corresponding author for this work

    Research output: Contribution to journalArticlepeer-review

    23 Citations (Scopus)

    Abstract

    Background: Plant immune proteins display complex conformations. Results: The Prf N-terminal domain forms a homo-dimer, has two binding sites for Pto kinase, and interacts with the Prf leucine-rich repeats domain. Conclusion: The Prf N-terminal domain coordinates multiple domain interactions to control the activity of the immune complex. Significance: Additional resolution is supplied to the Prf-Pto complex.

    Original languageEnglish
    Pages (from-to)11258-11267
    Number of pages10
    JournalJournal of Biological Chemistry
    Volume290
    Issue number18
    DOIs
    Publication statusPublished - 1 May 2015

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