5HYX
Plant peptide hormone receptor RGFR1 in complex with RGF1
Summary for 5HYX
| Entry DOI | 10.2210/pdb5hyx/pdb |
| Related | 5HZ0 5HZ1 5HZ3 |
| Descriptor | Probable LRR receptor-like serine/threonine-protein kinase At4g26540, PTR-SER-ASN-PRO-GLY-HIS-HIS-PRO-HYP-ARG-HIS-ASN, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total) |
| Functional Keywords | plant receptor, transferase |
| Biological source | Arabidopsis thaliana (Mouse-ear cress) More |
| Total number of polymer chains | 2 |
| Total formula weight | 71697.26 |
| Authors | |
| Primary citation | Song, W.,Liu, L.,Wang, J.,Wu, Z.,Zhang, H.,Tang, J.,Lin, G.,Wang, Y.,Wen, X.,Li, W.,Han, Z.,Guo, H.,Chai, J. Signature motif-guided identification of receptors for peptide hormones essential for root meristem growth Cell Res., 26:674-685, 2016 Cited by PubMed Abstract: Peptide-mediated cell-to-cell signaling has crucial roles in coordination and definition of cellular functions in plants. Peptide-receptor matching is important for understanding the mechanisms underlying peptide-mediated signaling. Here we report the structure-guided identification of root meristem growth factor (RGF) receptors important for plant development. An assay based on a signature ligand recognition motif (Arg-x-Arg) conserved in a subfamily of leucine-rich repeat receptor kinases (LRR-RKs) identified the functionally uncharacterized LRR-RK At4g26540 as a receptor of RGF1 (RGFR1). We further solved the crystal structure of RGF1 in complex with the LRR domain of RGFR1 at a resolution of 2.6 Å, which reveals that the Arg-x-Gly-Gly (RxGG) motif is responsible for specific recognition of the sulfate group of RGF1 by RGFR1. Based on the RxGG motif, we identified additional four RGFRs. Participation of the five RGFRs in RGF-induced signaling is supported by biochemical and genetic data. We also offer evidence showing that SERKs function as co-receptors for RGFs. Taken together, our study identifies RGF receptors and co-receptors that can link RGF signals with their downstream components and provides a proof of principle for structure-based matching of LRR-RKs with their peptide ligands. PubMed: 27229311DOI: 10.1038/cr.2016.62 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.596 Å) |
Structure validation
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