5GR9
Crystal structure of PXY-TDIF/CLE41
5GR9 の概要
| エントリーDOI | 10.2210/pdb5gr9/pdb |
| 分子名称 | Leucine-rich repeat receptor-like protein kinase TDR, TDIF/CLE41, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total) |
| 機能のキーワード | pxy, tdif, cle peptides, leucine rich repeat, transferase |
| 由来する生物種 | Arabidopsis thaliana (Mouse-ear cress) 詳細 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 69032.45 |
| 構造登録者 | |
| 主引用文献 | Zhang, H.Q.,Lin, X.Y.,Han, Z.F.,Qu, L.J.,Chai, J.J. Crystal structure of PXY-TDIF complex reveals a conserved recognition mechanism among CLE peptide-receptor pairs Cell Res., 26:543-555, 2016 Cited by PubMed Abstract: Plants can achieve amazing lifespans because of their continuous and repetitive formation of new organs by stem cells present within meristems. The balance between proliferation and differentiation of meristem cells is largely regulated by the CLAVATA3/ENDOSPERM SURROUNDING REGION (CLE) peptide hormones. One of the well-characterized CLE peptides, CLE41/TDIF (tracheary elements differentiation inhibitory factor), functions to suppress tracheary element differentiation and promote procambial cell proliferation, playing important roles in vascular development and wood formation. The recognition mechanisms of TDIF or other CLE peptides by their respective receptors, however, remain largely elusive. Here we report the crystal structure of TDIF in complex with its receptor PXY, a leucine-rich repeat receptor kinase (LRR-RK). Our structure reveals that TDIF mainly adopts an "Ω"-like conformation binding to the inner surface of the LRR domain of PXY. Interaction between TDIF and PXY is predominately mediated by the relatively conserved amino acids of TDIF. Structure-based sequence alignment showed that the TDIF-interacting motifs are also conserved among other known CLE receptors. Our data provide a structural template for understanding the recognition mechanism of CLE peptides by their receptors, offering an opportunity for the identification of receptors of other uncharacterized CLE peptides. PubMed: 27055373DOI: 10.1038/cr.2016.45 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.767 Å) |
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