3cig: Difference between revisions

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[[Image:3cig.~~jpg~~|left|200px]]

[[Image:3cig.png|left|200px]]

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~~'''~~Crystal structure of mouse TLR3 ectodomain~~'''~~

===Crystal structure of mouse TLR3 ectodomain===

~~==Overview==~~

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~~Toll~~-~~like receptor 3 (TLR3) recognizes double~~-~~stranded RNA (dsRNA)~~, ~~a molecular signature of most viruses~~, ~~and triggers inflammatory responses that prevent viral spread. TLR3 ectodomains~~ (~~ECDs) dimerize~~ on oligonucleotides of at least 40 to 50 base pairs in length, the minimal length required for signal transduction. To establish the molecular basis for ligand binding and signaling, we determined the crystal structure of a complex between two mouse TLR3-ECDs and dsRNA at 3.~~4 angstrom resolution~~. ~~Each TLR3-ECD binds dsRNA at two sites located at opposite ends of the TLR3 horseshoe~~, ~~and an intermolecular contact between the two TLR3-ECD C-terminal domains coordinates and stabilizes~~ the ~~dimer~~. ~~This juxtaposition could mediate downstream signaling by dimerizing the cytoplasmic Toll interleukin~~-~~1 receptor (TIR) domains. The overall shape of the TLR3~~-~~ECD does not change upon binding to dsRNA.~~

The line below this paragraph, {{ABSTRACT_PUBMED_18420935}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 18420935 is the PubMed ID number.

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==About this Structure==

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[[Category: Tlr]]

[[Category: Transmembrane]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Wed May 7 08~~:55:47 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 02:49:47 2008''

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-[[Image:3cig.jpg|left|200px]]
+{{Seed}}
+[[Image:3cig.png|left|200px]]
 <!--
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 {{STRUCTURE_3cig|  PDB=3cig  |  SCENE=  }}
-'''Crystal structure of mouse TLR3 ectodomain'''
+===Crystal structure of mouse TLR3 ectodomain===
-==Overview==
+<!--
-Toll-like receptor 3 (TLR3) recognizes double-stranded RNA (dsRNA), a molecular signature of most viruses, and triggers inflammatory responses that prevent viral spread. TLR3 ectodomains (ECDs) dimerize on oligonucleotides of at least 40 to 50 base pairs in length, the minimal length required for signal transduction. To establish the molecular basis for ligand binding and signaling, we determined the crystal structure of a complex between two mouse TLR3-ECDs and dsRNA at 3.4 angstrom resolution. Each TLR3-ECD binds dsRNA at two sites located at opposite ends of the TLR3 horseshoe, and an intermolecular contact between the two TLR3-ECD C-terminal domains coordinates and stabilizes the dimer. This juxtaposition could mediate downstream signaling by dimerizing the cytoplasmic Toll interleukin-1 receptor (TIR) domains. The overall shape of the TLR3-ECD does not change upon binding to dsRNA.
+The line below this paragraph, {{ABSTRACT_PUBMED_18420935}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 18420935 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_18420935}}
 ==About this Structure==
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 [[Category: Tlr]]
 [[Category: Transmembrane]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May  7 08:55:47 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 02:49:47 2008''