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Crystal structure of the plant receptor-like kinase TDR in complex with the TDIF peptide

Author

Listed:
  • Junko Morita

    (Graduate School of Science, The University of Tokyo)

  • Kazuki Kato

    (Graduate School of Science, The University of Tokyo)

  • Takanori Nakane

    (Graduate School of Science, The University of Tokyo)

  • Yuki Kondo

    (Graduate School of Science, The University of Tokyo)

  • Hiroo Fukuda

    (Graduate School of Science, The University of Tokyo)

  • Hiroshi Nishimasu

    (Graduate School of Science, The University of Tokyo
    JST, PRESTO)

  • Ryuichiro Ishitani

    (Graduate School of Science, The University of Tokyo)

  • Osamu Nureki

    (Graduate School of Science, The University of Tokyo)

Abstract

In plants, leucine-rich repeat receptor-like kinases (LRR-RKs) perceive ligands, including peptides and small molecules, to regulate various physiological processes. TDIF, a member of the CLE peptide family, specifically interacts with the LRR-RK TDR to inhibit meristem differentiation into tracheary elements, and promotes cell proliferation. Here we report the crystal structure of the extracellular domain of TDR in complex with the TDIF peptide. The extracellular domain of TDR adopts a superhelical structure comprising 22 LRRs, and specifically recognizes TDIF by its inner concave surface. Together with our biochemical and sequence analyses, our structure reveals a conserved TDIF-recognition mechanism of TDR among plant species. Furthermore, a structural comparison of TDR with other plant LRR-RKs suggested the activation mechanism of TDR by TDIF. The structure of this CLE peptide receptor provides insights into the recognition mechanism of the CLE family peptides.

Suggested Citation

  • Junko Morita & Kazuki Kato & Takanori Nakane & Yuki Kondo & Hiroo Fukuda & Hiroshi Nishimasu & Ryuichiro Ishitani & Osamu Nureki, 2016. "Crystal structure of the plant receptor-like kinase TDR in complex with the TDIF peptide," Nature Communications, Nature, vol. 7(1), pages 1-9, November.
    • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms12383
    DOI: 10.1038/ncomms12383
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