Sandbox Reserved 1718

From Proteopedia

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{{Template:CH462_Biochemistry_II_2022}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE -->
{{Template:CH462_Biochemistry_II_2022}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE -->
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==Your Heading Here (maybe something like 'Structure')==
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==Human Itch G-Protein Coupled Receptor==
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
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.
 
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== Function ==
 
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== Disease ==
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= Introduction =
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== Relevance ==
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== Function and Biological Role ==
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== Structural highlights ==
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=== Gq ===
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=== Gi ===
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== Significance of Human Itch GPCR ==
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nobel prize, methods of visualization, and the history of known diseases and their associated mutations
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== Related Enzymes ==
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X2 vs. X4
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= Structure =
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conserved domains and subunits: 7TM helices, etc.
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interactions with the Gq and Gi proteins
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== Active Site ==
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important residues
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the two binding pockets (electrostatics)
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difference between the binding pockets of X2 and X4; talk about why these differences affect the type of ligands that may bind
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== Substrates/Ligands ==
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Talk about there a ton of different ligands can bind
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Highlight the few that we want to talk about: Peptide vs. manufactured/artificial vs. non-peptide
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Agonists, inverse agonists, and antagonists and their effects on the mechanism
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== Mechanism ==
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mechanism of binding and the associated chemical interactions
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signaling cascades associated with the Human Itch GPCRs
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regulatory processes within the signaling cascade that directly affect the g-proteins
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= Relevance =
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== Implications for Disease ==
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significant mutations that have been found
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drug design for GPCR targeting
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== Clinical Relevance ==
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drug hypersensitivity article
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.
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.
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</StructureSection>
</StructureSection>
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article about drug hypersensitivity <ref>DOI: 10.3389/fimmu.2018.03027</ref>
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== References ==
== References ==
<references/>
<references/>

Revision as of 20:10, 15 March 2022

This Sandbox is Reserved from February 28 through September 1, 2022 for use in the course CH462 Biochemistry II taught by R. Jeremy Johnson at the Butler University, Indianapolis, USA. This reservation includes Sandbox Reserved 1700 through Sandbox Reserved 1729.
To get started:
  • Click the edit this page tab at the top. Save the page after each step, then edit it again.
  • show the Scene authoring tools, create a molecular scene, and save it. Copy the green link into the page.
  • Add a description of your scene. Use the buttons above the wikitext box for bold, italics, links, headlines, etc.

More help: Help:Editing

Human Itch G-Protein Coupled Receptor

Caption for this structure

Drag the structure with the mouse to rotate

article about drug hypersensitivity [1]

References

  1. Porebski G, Kwiecien K, Pawica M, Kwitniewski M. Mas-Related G Protein-Coupled Receptor-X2 (MRGPRX2) in Drug Hypersensitivity Reactions. Front Immunol. 2018 Dec 20;9:3027. doi: 10.3389/fimmu.2018.03027. eCollection, 2018. PMID:30619367 doi:http://dx.doi.org/10.3389/fimmu.2018.03027
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