8f7q: Difference between revisions
New page: '''Unreleased structure''' The entry 8f7q is ON HOLD Authors: Wang, Y., Zhuang, Y., DiBerto, J.F., Zhou, X.E., Schmitz, G.P., Yuan, Q., Jain, M.K., Liu, W., Melcher, K., Jiang, Y., Roth... |
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==Gi bound mu-opioid receptor in complex with beta-endorphin== | |||
<StructureSection load='8f7q' size='340' side='right'caption='[[8f7q]], [[Resolution|resolution]] 3.22Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8f7q]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus], [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens], [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8F7Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8F7Q FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.22Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CLR:CHOLESTEROL'>CLR</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8f7q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8f7q OCA], [https://pdbe.org/8f7q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8f7q RCSB], [https://www.ebi.ac.uk/pdbsum/8f7q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8f7q ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Opioids are effective analgesics, but their use is beset by serious side effects, including addiction and respiratory depression, which contribute to the ongoing opioid crisis. The human opioid system contains four opioid receptors (muOR, deltaOR, kappaOR, and NOPR) and a set of related endogenous opioid peptides (EOPs), which show distinct selectivity toward their respective opioid receptors (ORs). Despite being key to the development of safer analgesics, the mechanisms of molecular recognition and selectivity of EOPs to ORs remain unclear. Here, we systematically characterize the binding of EOPs to ORs and present five structures of EOP-OR-G(i) complexes, including beta-endorphin- and endomorphin-bound muOR, deltorphin-bound deltaOR, dynorphin-bound kappaOR, and nociceptin-bound NOPR. These structures, supported by biochemical results, uncover the specific recognition and selectivity of opioid peptides and the conserved mechanism of opioid receptor activation. These results provide a structural framework to facilitate rational design of safer opioid drugs for pain relief. | |||
Structures of the entire human opioid receptor family.,Wang Y, Zhuang Y, DiBerto JF, Zhou XE, Schmitz GP, Yuan Q, Jain MK, Liu W, Melcher K, Jiang Y, Roth BL, Xu HE Cell. 2023 Jan 19;186(2):413-427.e17. doi: 10.1016/j.cell.2022.12.026. Epub 2023 , Jan 12. PMID:36638794<ref>PMID:36638794</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 8f7q" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: Jain | ==See Also== | ||
[[Category: | *[[Opioid receptor|Opioid receptor]] | ||
[[Category: Liu | *[[Transducin 3D structures|Transducin 3D structures]] | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: Bos taurus]] | ||
[[Category: Yuan | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Rattus norvegicus]] | |||
[[Category: Synthetic construct]] | |||
[[Category: DiBerto JF]] | |||
[[Category: Jain MK]] | |||
[[Category: Jiang Y]] | |||
[[Category: Liu W]] | |||
[[Category: Melcher K]] | |||
[[Category: Roth BL]] | |||
[[Category: Schmitz GP]] | |||
[[Category: Wang Y]] | |||
[[Category: Xu HE]] | |||
[[Category: Yuan Q]] | |||
[[Category: Zhou XE]] | |||
[[Category: Zhuang Y]] | |||
Latest revision as of 12:51, 9 October 2024
Gi bound mu-opioid receptor in complex with beta-endorphinGi bound mu-opioid receptor in complex with beta-endorphin
Structural highlights
Publication Abstract from PubMedOpioids are effective analgesics, but their use is beset by serious side effects, including addiction and respiratory depression, which contribute to the ongoing opioid crisis. The human opioid system contains four opioid receptors (muOR, deltaOR, kappaOR, and NOPR) and a set of related endogenous opioid peptides (EOPs), which show distinct selectivity toward their respective opioid receptors (ORs). Despite being key to the development of safer analgesics, the mechanisms of molecular recognition and selectivity of EOPs to ORs remain unclear. Here, we systematically characterize the binding of EOPs to ORs and present five structures of EOP-OR-G(i) complexes, including beta-endorphin- and endomorphin-bound muOR, deltorphin-bound deltaOR, dynorphin-bound kappaOR, and nociceptin-bound NOPR. These structures, supported by biochemical results, uncover the specific recognition and selectivity of opioid peptides and the conserved mechanism of opioid receptor activation. These results provide a structural framework to facilitate rational design of safer opioid drugs for pain relief. Structures of the entire human opioid receptor family.,Wang Y, Zhuang Y, DiBerto JF, Zhou XE, Schmitz GP, Yuan Q, Jain MK, Liu W, Melcher K, Jiang Y, Roth BL, Xu HE Cell. 2023 Jan 19;186(2):413-427.e17. doi: 10.1016/j.cell.2022.12.026. Epub 2023 , Jan 12. PMID:36638794[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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