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PDBsum entry 5gij
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Signaling protein
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PDB id
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5gij
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References listed in PDB file
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Key reference
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Title
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Crystal structure of the plant receptor-Like kinase tdr in complex with the tdif peptide.
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Authors
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J.Morita,
K.Kato,
T.Nakane,
Y.Kondo,
H.Fukuda,
H.Nishimasu,
R.Ishitani,
O.Nureki.
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Ref.
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Nat Commun, 2016,
7,
12383.
[DOI no: ]
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PubMed id
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Abstract
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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.
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