Structural biology: Crystal structure of human toll-like receptor 3 (TLR3) ectodomain

Jungwoo Choe, Matthew S. Kelker, Ian A. Wilson

Research output: Contribution to journalArticlepeer-review

512 Scopus citations

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.

Original languageEnglish
Pages (from-to)581-585
Number of pages5
JournalScience
Volume309
Issue number5734
DOIs
StatePublished - 22 Jul 2005

Fingerprint

Dive into the research topics of 'Structural biology: Crystal structure of human toll-like receptor 3 (TLR3) ectodomain'. Together they form a unique fingerprint.

Cite this