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

Junko Morita, Kazuki Kato, Takanori Nakane, Yuki Kondo, Hiroo Fukuda, Hiroshi Nishimasu, Ryuichiro Ishitani () and Osamu Nureki ()
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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
Ryuichiro Ishitani: Graduate School of Science, The University of Tokyo
Osamu Nureki: Graduate School of Science, The University of Tokyo

Nature Communications, 2016, vol. 7, issue 1, 1-9

Abstract: 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.

Date: 2016
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DOI: 10.1038/ncomms12383

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