Sandbox GGC12: Difference between revisions
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== | ==Introduction== | ||
Toll-like Receptors are a part of a family of proteins that consist of ten type 1 transmembrane receptor proteins in human beings. Toll-like Receptor 11 is active in mice with a response to unropathogenic bacteria has been described as not functional in humans. Toll-like receptors that have evolved and are expressed in insects and higher animals. Toll-like receptor proteins mainly have two functional regions. The extracellular domain consists of leucine-rich repeats and one or two cysteine-rich regions that are recognized as an array of microbial components that include sugars, proteins, lipids, DNA motifs, and double-stranded RNA. The intracellular region does consist of a Toll/IL-1 receptor domain, which are like the intracellular domain of the IL-1 receptor. The Toll/IL-1 receptor domain it provides an intracellular scaffold their interacts with several adapter proteins that will initiate and integration as a well-defined signaling cascades resulting in a cellular activation, and the production of a number of cytokines and chemokines <ref>DOI 10.1016/B978-07216-3695-5.50016-X</ref> or to the article describing Jmol <ref>PMID:22579623</ref> to the rescue. | |||
Toll-like Receptors are a part of a family of proteins that consist of ten type 1 transmembrane receptor proteins in human beings. Toll-like Receptor 11 is active in mice with a response to unropathogenic bacteria has been described as not functional in humans. Toll-like receptors that have evolved and are expressed in insects and higher animals. Toll-like receptor proteins mainly have two functional regions. The extracellular domain consists of leucine-rich repeats and one or two cysteine-rich regions that are recognized as an array of microbial components that include sugars, proteins, lipids, DNA motifs, and double-stranded RNA. The intracellular region does consist of a Toll/IL-1 receptor domain, which are like the intracellular domain of the IL-1 receptor. The Toll/IL-1 receptor domain it provides an intracellular scaffold their interacts with several adapter proteins that will initiate and integration as a well-defined signaling cascades resulting in a cellular activation, and the production of a number of cytokines and chemokines <ref>DOI 10.1016/B978- | |||
== Function == | == Function == | ||
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TRIF pathway | TRIF pathway | ||
The various pathogens do target the signaling molecules and transcriptional regulators which are acting in the TRIF pathway, it goes on to demonstrate the main importance of this particular pathway which contributes to control of both viral and bacterial pathogens through a promotion of the inflammatory mediators and activators of antimicrobial responses. TRIF signaling also has both protective and pathologic roles in several chronic inflammatory disease conditions, as well as an essential function in wound‐repair processes <ref>DOI 10.1189/jlb.2RI1115-531R</ref>. | |||
TICAM1 | TICAM1 | ||
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== Structural highlights == | == Structural highlights == | ||
<scene name='78/781196/ | This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. <scene name='78/781196/Sec_structure/2'>This shows the secondary structure</scene> of Crystal Structure of Fab12. Here is a <scene name='78/781196/Ser212/10'>Zoomed in view</scene>name='78/781196/Ser212/2'>Zoomed out view</scene><scene name='78/781196/Ser212/1'>This is Ser212</scene> which is important | ||
</ | |||
</StructureSection> | |||
== References == | == References == | ||
<references/> | <references/> | ||
