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(Crystal structure of the µ-opioid receptor bound to a morphinan antagonist)
Current revision (01:03, 31 January 2018) (edit) (undo)
(Crystal structure of the µ-opioid receptor bound to a morphinan antagonist)
 
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<StructureSection load='' size='340' side='right' caption='Click a green link on the left to load Figure 1' scene=''>
<StructureSection load='' size='340' side='right' caption='Click a green link on the left to load Figure 1' scene=''>
'''Figure 1: Overall view of the µ-OR structure'''
'''Figure 1: Overall view of the µ-OR structure'''
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see [https://www.nature.com/articles/nature10954 the paper] for essentially this exact figure.
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Shown in <jmol><jmollink><text>Figure 1</text><script>exit;figure="http://proteopedia.org/wiki/images/2/20/Nature10954Fig1aLeft_4dkl-2.png";SCRIPT @figure</script></jmollink></jmol> is an overall view of the µ-opioid receptor bound to the morphinan antagonist ([https://chemapps.stolaf.edu/jmol/jmol.php?pdbid=BF0&script=set%20echo%20top%20left;echo%20PDBid%20BF0;spin%20on PDBid BF0]). The seven parallel trans-membrane helices are the signature of a "TM7" cell membrane receptor, spanning the 35-40 nm distance across the lipid bilayer of the cell.
Shown in <jmol><jmollink><text>Figure 1</text><script>exit;figure="http://proteopedia.org/wiki/images/2/20/Nature10954Fig1aLeft_4dkl-2.png";SCRIPT @figure</script></jmollink></jmol> is an overall view of the µ-opioid receptor bound to the morphinan antagonist ([https://chemapps.stolaf.edu/jmol/jmol.php?pdbid=BF0&script=set%20echo%20top%20left;echo%20PDBid%20BF0;spin%20on PDBid BF0]). The seven parallel trans-membrane helices are the signature of a "TM7" cell membrane receptor, spanning the 35-40 nm distance across the lipid bilayer of the cell.
At the top we see three extracellular loops, EC1, EC2, and EC3. Below, we see a short helix that is inside the cell.
At the top we see three extracellular loops, EC1, EC2, and EC3. Below, we see a short helix that is inside the cell.
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Notice that the inhibitor, shown as space-filling spheres, is nestled relatively deeply within the helical core. Binding at this position effects a change in conformation through a twisting action of the helices. This twisting gets delivered to a second binding site of the receptor. This second binding site is attached to the helical assembly via TM3 and TM6 (not shown here). It is where an associated protein that binds GTP can bind. This protein's binding is what makes this receptor a "G-protein-coupled receptor." Its binding triggers the transmission of the chemical "signal" delivered by the opioid (or, in this case, being prevented from doing that).
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Notice that the inhibitor, shown as space-filling spheres, is nestled relatively deeply within the helical core. Binding at this position effects a change in conformation through a twisting action of the helices. This twisting gets delivered to a second binding site of the receptor on the endocellular (inside the cell) side. This second binding site is attached to the helical assembly via TM3 and TM6 (not shown here). It is where an associated protein that binds GTP can bind. This protein's binding is what makes this receptor a "G-protein-coupled receptor." Its binding triggers the transmission of the chemical "signal" delivered by the opioid (or, in this case, being prevented from doing that).
Investigate the structure after loading the <jmol><jmollink><text>Figure 1 model</text><script>exit;SCRIPT "http://proteopedia.org/wiki/images/2/20/Nature10954Fig1aLeft_4dkl-2.png"</script></jmollink></jmol> by dragging it around using your mouse or clicking the buttons below. SHIFT-drag to zoom.
Investigate the structure after loading the <jmol><jmollink><text>Figure 1 model</text><script>exit;SCRIPT "http://proteopedia.org/wiki/images/2/20/Nature10954Fig1aLeft_4dkl-2.png"</script></jmollink></jmol> by dragging it around using your mouse or clicking the buttons below. SHIFT-drag to zoom.
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<jmol><jmollink><text>(a) exocellular view</text><script>SCRIPT http://proteopedia.org/wiki/images/0/00/Nature10954_fig1d.spt('top')</script></jmollink></jmol>
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<jmol><jmollink><text>(a) exocellular view</text><script>if (!figure){figure="http://proteopedia.org/wiki/images/2/20/Nature10954Fig1aLeft_4dkl-2.png";SCRIPT @figure}; SCRIPT http://proteopedia.org/wiki/images/0/00/Nature10954_fig1d.spt('top')</script></jmollink></jmol>
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<jmol><jmollink><text>(b) endocellular</text><script>SCRIPT http://proteopedia.org/wiki/images/0/00/Nature10954_fig1d.spt('bottom')</script></jmollink></jmol>
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<jmol><jmollink><text>(b) endocellular</text><script>if (!figure){figure="http://proteopedia.org/wiki/images/2/20/Nature10954Fig1aLeft_4dkl-2.png";SCRIPT @figure};SCRIPT http://proteopedia.org/wiki/images/0/00/Nature10954_fig1d.spt('bottom')</script></jmollink></jmol>
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<jmol><jmollink><text>(c) trans-membrane view</text><script>SCRIPT http://proteopedia.org/wiki/images/0/00/Nature10954_fig1d.spt('side')</script></jmollink></jmol>
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<jmol><jmollink><text>(c) trans-membrane view</text><script>if (!figure){figure="http://proteopedia.org/wiki/images/2/20/Nature10954Fig1aLeft_4dkl-2.png";SCRIPT @figure};SCRIPT http://proteopedia.org/wiki/images/0/00/Nature10954_fig1d.spt('side')</script></jmollink></jmol>
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<jmol><jmollink><text>(d) trans-membrane view with abstract membrane</text><script>SCRIPT http://proteopedia.org/wiki/images/0/00/Nature10954_fig1d.spt('draw')</script></jmollink></jmol>
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<jmol><jmollink><text>(d) trans-membrane view with abstract membrane</text><script>if (!figure){figure="http://proteopedia.org/wiki/images/2/20/Nature10954Fig1aLeft_4dkl-2.png";SCRIPT @figure};SCRIPT http://proteopedia.org/wiki/images/0/00/Nature10954_fig1d.spt('draw')</script></jmollink></jmol>
</StructureSection>
</StructureSection>
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<jmol><jmollink><text>Animate Figure 1a</text><script>script "http://proteopedia.org/wiki/images/1/1f/Nature10954_fig1a.spt"</script></jmollink></jmol>
 
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/wiki/images/8/8b/4dkl-local-contact.png
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BELOW THIS LINE IS NOT PART OF THE ACTUAL PAGE
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code for the above (space inserted just after the : <code>&lt;jmol><jmollink><text>View Figure 1a: Overall view of the µ-OR structure</text><script>exit;figure=1;SCRIPT "/wiki/images/8/8b/4dkl-local-contact.png"</script></jmollink></jmol></code>
code for the above (space inserted just after the : <code>&lt;jmol><jmollink><text>View Figure 1a: Overall view of the µ-OR structure</text><script>exit;figure=1;SCRIPT "/wiki/images/8/8b/4dkl-local-contact.png"</script></jmollink></jmol></code>
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<jmol><jmollink><text>Animate Figure 1a</text><script>script "http://proteopedia.org/wiki/images/1/1f/Nature10954_fig1a.spt"</script></jmollink></jmol>
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Current revision

Crystal structure of the µ-opioid receptor bound to a morphinan antagonist

[https://www.nature.com/articles/nature10954 Nature volume 485, pages 321–326 (17 May 2012) doi:10.1038/nature10954]

Click a green link on the left to load Figure 1

Drag the structure with the mouse to rotate


BELOW THIS LINE IS NOT PART OF THE ACTUAL PAGE

code for the above (space inserted just after the : <jmol><jmollink><text>View Figure 1a: Overall view of the µ-OR structure</text><script>exit;figure=1;SCRIPT "/wiki/images/8/8b/4dkl-local-contact.png"</script></jmollink></jmol>





is a close-up view of a  bound to the µ-opioid receptor. The green circles indicate hydrogen bonds. 
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