Article
Analysis of TLR4 polymorphic variants: new insights into TLR4/MD-2/CD14 stoichiometry, structure, and signaling.
Journal of immunology (Baltimore, Md. : 1950) - 1 Jul 2006
Rallabhandi Prasad, Bell Jessica, Boukhvalova Marina S, Medvedev Andrei, Lorenz Eva, Arditi Moshe, Hemming Val G, Blanco Jorge C G, Segal David M, Vogel Stefanie N
Abstract excerpt
TLR4 is the signal-transducing receptor for structurally diverse microbial molecules such as bacterial LPS, respiratory syncytial virus fusion (F) protein, and chlamydial heat shock protein 60. Previous studies associated two polymorphic mutations in the extracellular domain of TLR4 (Asp(299)Gly and Thr(399)Ile) with decreased LPS responsiveness. To analyze the molecular basis for diminished responsiveness,...
Topics
- Amino Acid Substitution
- Aspartic Acid
- Cell Line
- Extracellular Space
- Genetic Variation
- Glycine
- Humans
- Isoleucine
- Lipopolysaccharide Receptors
- Lipopolysaccharides
- Lymphocyte Antigen 96
- Oligopeptides
- Peptides