期刊
SCIENCE
卷 309, 期 5734, 页码 581-585出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1115253
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资金
- NCI NIH HHS [CA-58896] Funding Source: Medline
- NIAID NIH HHS [AI-42266, R01 AI042266, T32 AI077606] Funding Source: Medline
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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