
Health Dictionary
Reliable, easy-to-read patient information on common medical conditions — written in plain language, free of jargon, and grounded in current evidence. Browse the most frequent diagnoses, understand what they mean for everyday life, and learn which steps and questions help you have a focused conversation with your doctor.
TLR 3
Introduction
TLR 3 is a member of the Toll-like receptor family of pattern recognition receptors of the innate immune system. Discovered in 2001,[1] TLR3 recognizes double-stranded RNA, a form of genetic information carried by some viruses such as influenza. Upon recognition, TLR 3 induces the activation of NF-kB to increase production of type I interferons which signal other cells to increase their antiviral defenses. Double-stranded RNA is also recognised by the cytoplasmic receptors RIG-I and MDA-5.
Structure
Structure
The structure of TLR3 was reported in June 2005 by researchers at The Scripps Research Institute.[2] TLR3 forms a large horseshoe shape that contacts with a neighboring horseshoe, forming a “dimer” of two horseshoes. Much of the TLR3 protein surface is covered with sugar molecules, making it a glycoprotein, but on one face (including the interface between the two horseshoes), there is a large sugar-free surface. This surface also contains two distinct patches rich in positively-charged amino acids, which may be a binding site for negatively-charged double-stranded RNA.
Despite being a glycoprotein, TLR3 crystallises readily – a prerequisite for structural analysis by x-ray crystallography.
References
References
- ↑ Alexopoulou L, Holt A, Medzhitov R, Flavell R (2001). “Recognition of double-stranded RNA and activation of NF-kappaB by Toll-like receptor 3”. Nature. 413 (6857): 732–8. PMID 11607032.
- ↑ Choe J, Kelker M, Wilson I (2005). “Crystal structure of human toll-like receptor 3 (TLR3) ectodomain”. Science. 309 (5734): 581–5. PMID 15961631.
