8SUF
The complex of TOL-1 ectodomain bound to LAT-1 Lectin domain
8SUF の概要
| エントリーDOI | 10.2210/pdb8suf/pdb |
| 分子名称 | TIR domain-containing protein, Latrophilin-like protein 1, alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (8 entities in total) |
| 機能のキーワード | cell surface receptor, cell adhesion |
| 由来する生物種 | Caenorhabditis elegans 詳細 |
| タンパク質・核酸の鎖数 | 8 |
| 化学式量合計 | 507337.26 |
| 構造登録者 | |
| 主引用文献 | Carmona-Rosas, G.,Li, J.,Smith, J.J.,Nawrocka, W.I.,Cheng, S.,Baltrusaitis, E.E.,Zhao, M.,Arac, D.,Kratsios, P.,Ozkan, E. Structural basis and functional roles for Toll-like receptor binding to Latrophilin in C. elegans development. Nat.Struct.Mol.Biol., 32:1683-1696, 2025 Cited by PubMed Abstract: Latrophilins are conserved adhesion-type G-protein-coupled receptors associated with embryonic defects and lethality. However, their mechanistic roles and ligands in embryogenesis remain unknown. Here, we identified TOL-1, the sole Toll-like receptor in Caenorhabditis elegans, as a ligand for the C. elegans latrophilin, LAT-1. The extracellular lectin domain of LAT-1 directly binds to the second leucine-rich repeat domain of TOL-1. The crystal structure and cryo-electron microscopy density map of the LAT-1-TOL-1 extracellular region complex reveal a one-to-one lectin domain interaction with the convex face of a leucine-rich repeat domain. In C. elegans, endogenous mRNA and protein localization analyses showed mutually exclusive sites of expression, suggesting that in vivo LAT-1-TOL-1 interactions mostly occur in trans. Mutagenesis of key interface residues that disrupt the LAT-1-TOL-1 interaction led to partial lethality and malformed embryos. Thus, TOL-1 binding to LAT-1 represents a receptor-ligand axis essential for animal development. PubMed: 40588662DOI: 10.1038/s41594-025-01592-8 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (4 Å) |
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