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Crystal structure of human toll-like receptor 3 (tlr3) ectodomain

Academic Article
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Overview

related to degree

  • Kelker, Matthew, Ph.D. in Biophysics, Scripps Research 2000 - 2005

authors

  • Choe, J.
  • Kelker, Matthew
  • Wilson, Ian

publication date

  • July 2005

journal

  • Science  Journal

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.

subject areas

  • Amino Acid Motifs
  • Amino Acid Sequence
  • Binding Sites
  • Crystallography, X-Ray
  • Dimerization
  • Glycosylation
  • Humans
  • Hydrogen Bonding
  • Leucine
  • Ligands
  • Membrane Glycoproteins
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Conformation
  • Protein Structure, Tertiary
  • RNA, Double-Stranded
  • Receptors, Cell Surface
  • Repetitive Sequences, Amino Acid
  • Signal Transduction
  • Static Electricity
  • Surface Properties
  • Toll-Like Receptor 3
  • Toll-Like Receptors
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Identity

International Standard Serial Number (ISSN)

  • 0036-8075

Digital Object Identifier (DOI)

  • 10.1126/science.1115253

PubMed ID

  • 15961631
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Additional Document Info

start page

  • 581

end page

  • 585

volume

  • 309

issue

  • 5734

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