2A0Z

The molecular structure of toll-like receptor 3 ligand binding domain

Summary for 2A0Z

• Entry DOI: 10.2210/pdb2a0z/pdb
• Descriptor: Toll-like receptor 3, BETA-MERCAPTOETHANOL, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (11 entities in total)
• Functional Keywords: leucine rich repeat, solenoid, glycosylation, tlr3, immune system
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 86447.81

Authors

Bell, J.K.,Botos, I.,Hall, P.R.,Askins, J.,Shiloach, J.,Segal, D.M.,Davies, D.R. (deposition date: 2005-06-17, release date: 2005-08-02, Last modification date: 2025-03-26)

Primary citation

Bell, J.K.,Botos, I.,Hall, P.R.,Askins, J.,Shiloach, J.,Segal, D.M.,Davies, D.R.
The molecular structure of the Toll-like receptor 3 ligand-binding domain
Proc.Natl.Acad.Sci.USA, 102:10976-10980, 2005

PubMed Abstract: Innate immunity is the first line of defense against invading pathogens. Toll-like receptors (TLRs) act as sentinels of the innate immune system, sensing a variety of ligands from lipopolysaccharide to flagellin to dsRNA through their ligand-binding domain that is composed of leucine-rich repeats (LRRs). Ligand binding initiates a signaling cascade that leads to the up-regulation of inflammation mediators. In this study, we have expressed and crystallized the ectodomain (ECD) of human TLR3, which recognizes dsRNA, a molecular signature of viruses, and have determined the molecular structure to 2.4-A resolution. The overall horseshoe-shaped structure of the TLR3-ECD is formed by 23 repeating LRRs that are capped at each end by specialized non-LRR domains. The extensive beta-sheet on the molecule's concave surface forms a platform for several modifications, including insertions in the LRRs and 11 N-linked glycans. The TLR3-ECD structure indicates how LRR loops can establish distinct pathogen recognition receptors.

PubMed: 16043704
DOI: 10.1073/pnas.0505077102

Experimental method

X-RAY DIFFRACTION (2.4 Å)