Crystal Structure of Human Toll-Like Receptor 3 (TLR3) Ectodomain
摘要：
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.
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关键词：
DOUBLE-STRANDED-RNA LEUCINE-RICH REPEAT NF-KAPPA-B GLYCOPROTEIN IB-ALPHA RIBONUCLEASE INHIBITOR CYTOPLASMIC DOMAIN INNATE IMMUNITY CUTTING EDGE PROTEIN RECOGNITION
DOI：
10.1126/science.1115253
被引量：
年份：
2005
doi.org
掌桥科研
万方医学
Cell Press
NCBI
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