Sandbox GGC12

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==Crystal Structure of Fab12==
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==Your Heading Here (maybe something like 'Structure')==
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<StructureSection load='3ULS' size='340' side='right' caption='Crystal Structure of Fab12' scene=''>
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<StructureSection load='3VEV' size='340' side='right' caption='Caption for this structure' scene=''>
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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-O7216-3695-5.50016-X</ref> or to the article describing Jmol <ref>PMID:22579623</ref> to the rescue.
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This is a default text for your page. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
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You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
== Function ==
== Function ==
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Controls the host immune response system against any pathogens through the recognition of molecular patterns tahat are specific to each microorganism. TLR3 is a nuclear-sensing TLR which is going to be essentially activated by a double-stranded RNA, which is a sign of a viral infection. Acts via the adapter TRIF/TICAM1, that leads to a NF-kappa-B activation, IRF3 nuclear translocation, cytokine secretion and the inflammatory response <ref>PMID:12471095</ref>.
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== Disease ==
== Disease ==
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A rare complication of human herpesvirus 1 (HHV-1) infection, it occurs in only a small minority of HHV-1 infected individuals. There are characterized by a hemorrhagic necrosis of parts from both the temporal and frontal lobes. One of the onsets are that it invloves several days of fear, headache, seizures, stupor, and often coma, frequently with a fatal outcome <ref>PMID:17872438</ref>.
 
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== Relevance ==
 
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TRIF pathway
 
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Various of the 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>.
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== Relevance ==
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TICAM1
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It is involved in an innate immunity against invading pathogens. The main adapter used by TLR3, TLR4 (through TICAM2) and TLR5 to mediate the NF-kappa-B and interferon-regulatory factor (IRF) activation, and they go on to induce apoptosis. Ligand binding for these receptors would result in TRIF recruitment through its TIR domain. It is a quite distinct protein-interaction motif which allows a recruitment of the effector proteins TBK1, TRAF6 and RIPK1, which in turn, leads to the activation of transcription factors IRF3 and IRF7, NF-kappa-B and FADD respectively. Phosphorylation by TBK1 on the pLxIS motif will lead to recruitments and subsequent activation of the transcription factor IRF3 to induce expression of type I interferon and exert a potent immunity against invading pathogens. With the component of a multi-helicase-TICAM1 complex which will act as a cytoplasmic sensor of viral double-stranded RNA (dsRNA) and it plays a significant role in the activation of a cascade of antiviral responses including the induction of proinflammatory cytokines. Ubiquitously expressed but with higher levels in liver <ref>DOI 10.1016/j.jmb.2013.11.024</ref>.
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IRF3
 
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Transcriptional regulator of type I interferon (IFN)-dependent immune responses which plays a critical role with the innate immune response against DNA and RNA viruses. It will occssionally regulate the transcription of type I IFN genes (IFN-alpha and IFN-beta) and IFN-stimulated genes (ISG) by binding to an interferon-stimulated response element (ISRE) with their promoters. It would act as a more potent activator of the IFN-beta (IFNB) gene than the IFN-alpha (IFNA) gene and plays a critical and significant role in both the early and late phases of the IFNA/B gene induction. There are going to be found in an inactive form within the cytoplasm of uninfected cells and following the viral infection, double-stranded RNA (dsRNA), or toll-like receptor (TLR) signaling, is going to be phosphorylated by IKBKE and TBK1 kinases. There are going to induce a conformational change, leading to its dimerization and nuclear localization and association with CREB binding protein (CREBBP) to form dsRNA-activated factor 1 (DRAF1), a complex which activates the transcription of the type I IFN and ISG genes. Can activate distinct gene expression programs in macrophages and can induce significant apoptosis in primary macrophages <ref>DOI 10.1038/nri3581</ref> <ref>DOI 10.1016/j.coviro.2011.11.001</ref>.
 
== Structural highlights ==
== Structural highlights ==
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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
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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.
</StructureSection>
</StructureSection>
== References ==
== References ==
<references/>
<references/>

Revision as of 15:17, 10 February 2021

Your Heading Here (maybe something like 'Structure')

Caption for this structure

Drag the structure with the mouse to rotate

References

  1. Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
  2. Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
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