4ARN

Crystal structure of the N-terminal domain of Drosophila Toll receptor

4ARN の概要

• エントリーDOI: 10.2210/pdb4arn/pdb
• 分子名称: TOLL RECEPTOR, VARIABLE LYMPHOCYTE RECEPTOR B.61 CHIMERA, alpha-L-fucopyranose-(1-6)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total)
• 機能のキーワード: immune system, cytokine receptor, embryonic development, innate immunity, leucine-rich repeat, lrr hybrid technology
• 由来する生物種: DROSOPHILA MELANOGASTER (FRUIT FLY); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 131560.74

構造登録者

Gangloff, M.,Gay, N.J. (登録日: 2012-04-25, 公開日: 2013-01-23, 最終更新日: 2024-11-06)

主引用文献

Gangloff, M.,Arnot, C.J.,Lewis, M.,Gay, N.J.
Functional Insights from the Crystal Structure of the N-Terminal Domain of the Prototypical Toll Receptor.
Structure, 21:143-, 2013

PubMed Abstract: Drosophila melanogaster Toll is the founding member of an important family of pathogen-recognition receptors in humans, the Toll-like receptor (TLR) family. In contrast, the prototypical receptor is a cytokine-like receptor for Spätzle (Spz) protein and plays a dual role in both development and immunity. Here, we present the crystal structure of the N-terminal domain of the receptor that encompasses the first 201 amino acids at 2.4 Å resolution. To our knowledge, the cysteine-rich cap adopts a novel fold unique to Toll-1 orthologs in insects and that is not critical for ligand binding. However, we observed that an antibody directed against the first ten LRRs blocks Spz signaling in a Drosophila cell-based assay. Supplemented by point mutagenesis and deletion analysis, our data suggests that the region up to LRR 14 is involved in Spz binding. Comparison with mammalian TLRs reconciles previous contradictory findings about the mechanism of Toll activation.

PubMed: 23245851
DOI: 10.1016/J.STR.2012.11.003

実験手法

X-RAY DIFFRACTION (2.41 Å)