5gij | pdb_00005gij

Crystal structure of TDR-TDIF complex

spinqualitylabelsall models 5gij, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5gij is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: FUC, MAN, NAG NonStd Res: HYP Activity: Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [TDR_ARATH] Acts with CLE41p and CLE44p peptides as a ligand-receptor pair in a signal transduction pathway involved in the regulation of procambium maintenance and polarity during vascular-tissue development. Mediates repression of tracheary element differentiation and the promotion of procambial cells formation and polar division adjacent to phloem cells in the veins. [CLE41_ARATH] Extracellular signal peptide that regulates cell fate. May act with TDR as a ligand-receptor pair in a signal transduction pathway that represses tracheary element differentiation but promotes the formation of procambial cells adjacent to phloem cells in the veins in an auxin-dependent manner. Publication Abstract from PubMed 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. Crystal structure of the plant receptor-like kinase TDR in complex with the TDIF peptide.,Morita J, Kato K, Nakane T, Kondo Y, Fukuda H, Nishimasu H, Ishitani R, Nureki O Nat Commun. 2016 Aug 8;7:12383. doi: 10.1038/ncomms12383. PMID:27498761 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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