Sandbox WWC2: Difference between revisions

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''Hello World''! Welcome to my '''Proteopedia''' page.
==Your Heading Here (maybe something like 'Structure')==
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page '''Sandbox WWC2'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
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.


The µ-Opioid receptor
== Function ==


Opioids are highly specific in function and bind to a family of receptor proteins known as the opioid receptors (OR) µ-, κ-, δ-, respectively. The µ-OR, exists in the brain, spinal cord, and in the periphery and belongs to the protein superfamily G-protein coupled receptors (GCPRs). This transmembrane protein is composed of 7 membrane-spanning alpha-helical structures in which the extracellular ligand binding pocket exists. The µ-OR crystalized is that of the Mus musculus and has been assigned the protein database (PDB) identification 4DKL. This protein was crystalized on a 2.8 Å resolution with a bound irreversible morphinan antagonist β-funaltrexamine (β-FNA) (Manglik et al., 2012). This protein was crystalyzed with the addition of a T-4 lysozyme to permit stability of the 7 TM helices by Manglik et al in 2012. Interacting residues with known ligands in the binding pocket have been determined by Cui et al in 2013, and correlate with the previously mentioned binding pocket.
== Disease ==


== Relevance ==


== Structural highlights ==


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.


<Structure load='4dkl' size='800' frame='true' align='right' caption='''Mus musculus'' mu-OR' scene='Insert optional scene name here' />
</StructureSection>
<scene name='69/696303/4dkl_polar_meshribbon/2'>Polar mesh-ribbon view</scene>
== References ==
 
<references/>
 
<Structure load='4dkl' size='500' frame='true' align='right_bottom' caption='Insert caption here' scene='Insert optional scene name here' />
 
[[Image:MW_Folding_Simulations.gif]]
 
 
<quiz display=simple>
{How many α-helices compose the binding pocket?
|type="[]"}
- None.
- Nine.
- Four.
+ Seven.
</quiz>

Revision as of 20:52, 25 March 2016

Your Heading Here (maybe something like 'Structure')Your Heading Here (maybe something like 'Structure')

This is a default text for your page Sandbox WWC2. Click above on edit this page to modify. Be careful with the < and > signs.

You may include any references to papers as in: the use of JSmol in Proteopedia [1] or to the article describing Jmol [2] to the rescue.

Function

Disease

Relevance

Structural highlights

This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.


Caption for this structure

Drag the structure with the mouse to rotate

ReferencesReferences

  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

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Dana Emmert, Evan Muir
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