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Crystal Structure of Human Toll-Like Receptor 3 (TLR3) Ectodomain
Jungwoo Choe,Matthew S. Kelker,Ian A. Wilson*
Toll-like receptors (TLRs) play key roles in activating immuneresponses during infection. The human TLR3 ectodomain structureat 2.1 angstroms reveals a large horseshoe-shaped solenoid assembledfrom 23 leucine-rich repeats (LRRs). Asparagines conserved inthe 24-residue LRR motif contribute extensive hydrogen-bondingnetworks for solenoid stabilization. TLR3 is largely maskedby carbohydrate, but one face is glycosylation-free, which suggestsits potential role in ligand binding and oligomerization. Highlyconserved surface residues and a TLR3-specific LRR insertionform a homodimer interface in the crystal, whereas two patchesof positively charged residues and a second insertion wouldprovide an appropriate binding site for double-stranded RNA.
Department of Molecular Biology and The Skaggs Institute for Chemical Biology, The Scripps Research Institute (TSRI), 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
Published online 16 June 2005
Include this information when citing this paper.
* To whom correspondence should be addressed. E-mail: wilson{at}scripps.edu
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