TLR 3 Information & TLR 3 Links at HealthHaven.com

Toll-like receptor 3
	The structure of TLR3 covered with sugars
Available structures
	1ziw, 2a0z
Identifiers
Symbols	TLR3; CD283
External IDs	OMIM: 603029 MGI: 2156367 HomoloGene: 20696
Gene ontology
Molecular function	• double-stranded RNA binding; • transmembrane receptor activity; • protein binding;
Cellular component	• integral to plasma membrane; • membrane;
Biological process	• inflammatory response; • hyperosmotic response; • signal transduction; • activation of NF-kappaB-inducing kinase; • detection of virus; • defense response to bacterium; • positive regulation of I-kappaB kinase/NF-kappaB cascade; • positive regulation of interferon-gamma biosynthetic process; • innate immune response; • positive regulation of interferon-alpha biosynthetic process; • positive regulation of interferon-beta biosynthetic process; • negative regulation of osteoclast differentiation; • positive regulation of JNK cascade;
RNA expression pattern
	More reference expression data
Orthologs
NP_003256 (protein)	NP_569054 (protein)

edit

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 reoviruses. 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. TLR3 has also been designated as CD283 (cluster of differentiation 283).

[edit] 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 proposed 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.

[edit] References

^ Alexopoulou L, Holt AC, Medzhitov R, Flavell RA (2001). "Recognition of double-stranded RNA and activation of NF-kappaB by Toll-like receptor 3". Nature 413 (6857): 732–8. doi:10.1038/35099560. PMID 11607032.
^ Choe J, Kelker MS, Wilson IA (2005). "Crystal structure of human toll-like receptor 3 (TLR3) ectodomain". Science 309 (5734): 581–5. doi:10.1126/science.1115253. PMID 15961631.

[edit] Further reading

Lien E, Ingalls RR (2002). "Toll-like receptors.". Crit. Care Med. 30 (1 Suppl): S1–11. doi:10.1097/00003246-200201001-00001. PMID 11782555.

[pmid11607032-0] Alexopoulou L, Holt AC, Medzhitov R, Flavell RA (2001). "Recognition of double-stranded RNA and activation of NF-kappaB by Toll-like receptor 3". Nature 413 (6857): 732–8. doi:10.1038/35099560. PMID 11607032.

[pmid15961631-1] Choe J, Kelker MS, Wilson IA (2005). "Crystal structure of human toll-like receptor 3 (TLR3) ectodomain". Science 309 (5734): 581–5. doi:10.1126/science.1115253. PMID 15961631.

[1]

[2]