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(→Crystal structure of the µ-opioid receptor bound to a morphinan antagonist)
(→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=''>
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'''Figure 1: Overall view of the µ-OR structure'''
'''Figure 1: Overall view of the µ-OR structure'''
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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.
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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).
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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Investigate the structure by dragging it around using your mouse or clicking the buttons below.
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Investigate the structure by dragging it around using your mouse or clicking the buttons below. Press SHIFT to zoom.
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<jmol><jmollink><text>(a) Side view</text><script>SCRIPT http://proteopedia.org/wiki/images/c/ca/Nature10954_fig1b.spt('side')</script></jmollink></jmol>
<jmol><jmollink><text>(a) Side view</text><script>SCRIPT http://proteopedia.org/wiki/images/c/ca/Nature10954_fig1b.spt('side')</script></jmollink></jmol>
<jmol><jmollink><text>(b) Top view</text><script>SCRIPT http://proteopedia.org/wiki/images/c/ca/Nature10954_fig1b.spt('top')</script></jmollink></jmol>
<jmol><jmollink><text>(b) Top view</text><script>SCRIPT http://proteopedia.org/wiki/images/c/ca/Nature10954_fig1b.spt('top')</script></jmollink></jmol>
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<jmol><jmollink><text>(c) Bottom view</text><script>SCRIPT http://proteopedia.org/wiki/images/c/ca/Nature10954_fig1b.spt('bottom')</script></jmollink></jmol>
<jmol><jmollink><text>(c) Bottom view</text><script>SCRIPT http://proteopedia.org/wiki/images/c/ca/Nature10954_fig1b.spt('bottom')</script></jmollink></jmol>
<jmol><jmollink><text>(d) Side view with abstract membrane</text><script>SCRIPT http://proteopedia.org/wiki/images/c/ca/Nature10954_fig1b.spt('draw')</script></jmollink></jmol>
<jmol><jmollink><text>(d) Side view with abstract membrane</text><script>SCRIPT http://proteopedia.org/wiki/images/c/ca/Nature10954_fig1b.spt('draw')</script></jmollink></jmol>
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</StructureSection>
</StructureSection>

Revision as of 02:19, 30 January 2018

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

Please note this way for referencing a paper using the PubmedID [1]. The full reference appears at the bottom of the page.

[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

/wiki/images/8/8b/4dkl-local-contact.png 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.
  1. ↑ Manglik A, Kruse AC, Kobilka TS, Thian FS, Mathiesen JM, Sunahara RK, Pardo L, Weis WI, Kobilka BK, Granier S. Crystal structure of the micro-opioid receptor bound to a morphinan antagonist. Nature. 2012 Mar 21. doi: 10.1038/nature10954. PMID:22437502 doi:10.1038/nature10954
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