Two Modes of Ligand Recognition by Tlrs.
From: Howard Hughes Medical Institute and Section of Immunobiology, Yale University School of Medicine, New Haven, CT 06520, USA. igor.brodsky@yale.edu
Cell
- Publish Date: Sep 2007
- ISSN: 0092-8674
- Volume: 130
- Issue: 6
- Pages: 979-81
- Medium: Print
- Language: English
- Citation (JAMA): Brodsky Igor, Medzhitov Ruslan, et al. Two Modes of Ligand Recognition by Tlrs.. Cell Sep 2007;130:979-81
Abstract
Toll-like receptors (TLRs) are membrane-bound sensors that detect and respond to microbial infection. Two studies in Cell, one in this issue, reveal how TLRs recognize their ligands. Kim et al. (2007) recently reported the structure of TLR4 bound to the accessory protein MD-2 and its antagonist, the drug eritoran. In this issue, Jin et al. (2007) describe the crystal structure of a complex between TLR1, TLR2, and a lipopeptide ligand.
Mesh Headings (Keywords): Animals, Binding Sites, Crystallography, Dimerization, Disaccharides, Humans, Hydrogen Bonding, Hydrophobicity, Immunity, Natural, Ligands, Lipopolysaccharides, Lymphocyte Antigen 96, Mice, Molecular Structure, Peptides, Protein Binding, Protein Conformation, Signal Transduction, Sugar Phosphates, Toll-Like Receptor 1, Toll-Like Receptor 2, Toll-Like Receptor 4, Toll-Like Receptor 6
Check for Full Text / PubMed Unique Identifier (PMID): 17889640
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