Abstract
Toll-like receptors (TLRs) play key roles in activating immune responses during infection. The human TLR3 ectodomain structure at 2.1 angstroms reveals a large horseshoe-shaped solenoid assembled from 23 leucine-rich repeats (LRRs). Asparagines conserved in the 24-residue LRR motif contribute extensive hydrogen-bonding networks for solenoid stabilization. TLR3 is largely masked by carbohydrate, but one face is glycosylation-free, which suggests its potential role in ligand binding and oligomerization. Highly conserved surface residues and a TLR3-specific LRR insertion form a homodimer interface in the crystal, whereas two patches of positively charged residues and a second insertion would provide an appropriate binding site for double-stranded RNA.
Keywords
EctodomainTLR3ChemistryLeucine-rich repeatReceptorCell biologyToll-like receptorBiologyInnate immune systemBiochemistry
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Publication Info
- Year
- 2005
- Type
- article
- Volume
- 309
- Issue
- 5734
- Pages
- 581-585
- Citations
- 577
- Access
- Closed
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Cite This
Jungwoo Choe,
Matthew S. Kelker,
Ian A. Wilson
(2005).
Crystal Structure of Human Toll-Like Receptor 3 (TLR3) Ectodomain.
Science
, 309
(5734)
, 581-585.
https://doi.org/10.1126/science.1115253
Identifiers
- DOI
- 10.1126/science.1115253