8dwc

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Current revision (09:34, 17 October 2024) (edit) (undo)
 
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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[8dwc]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus], [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8DWC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8DWC FirstGlance]. <br>
<table><tr><td colspan='2'>[[8dwc]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus], [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8DWC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8DWC FirstGlance]. <br>
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</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=8dwc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8dwc OCA], [https://pdbe.org/8dwc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8dwc RCSB], [https://www.ebi.ac.uk/pdbsum/8dwc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8dwc ProSAT]</span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.87&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8dwc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8dwc OCA], [https://pdbe.org/8dwc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8dwc RCSB], [https://www.ebi.ac.uk/pdbsum/8dwc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8dwc ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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<div style="background-color:#fffaf0;">
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[https://www.uniprot.org/uniprot/PENK_BOVIN PENK_BOVIN] Neuropeptide that competes with and mimic the effects of opiate drugs. They play a role in a number of physiologic functions, including pain perception and responses to stress.[UniProtKB:P01210] Neuropeptide that competes with and mimic the effects of opiate drugs. They play a role in a number of physiologic functions, including pain perception and responses to stress.[UniProtKB:P01210] Met-enkephalin-Arg-Phe neuropeptide acts as a strong ligand of Mu-type opioid receptor OPRM1. Met-enkephalin-Arg-Phe-binding to OPRM1 in the nucleus accumbens of the brain increases activation of OPRM1, leading to long-term synaptic depression of glutamate release.[UniProtKB:P22005] Increases glutamate release in the striatum and decreases GABA concentration in the striatum.[UniProtKB:P04094] Increases glutamate release in the striatum.[UniProtKB:P04094] Enkelytin possesses antibacterial activity against Gram-positive bacteria such as Micrococcus luteus and Bacillus megaterium.<ref>PMID:8654396</ref>
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== Publication Abstract from PubMed ==
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The human MAS-related G protein-coupled receptor X1 (MRGPRX1) is preferentially expressed in the small-diameter primary sensory neurons and involved in the mediation of nociception and pruritus. Central activation of MRGPRX1 by the endogenous opioid peptide fragment BAM8-22 and its positive allosteric modulator ML382 has been shown to effectively inhibit persistent pain, making MRGPRX1 a promising target for non-opioid pain treatment. However, the activation mechanism of MRGPRX1 is still largely unknown. Here we report three high-resolution cryogenic electron microscopy structures of MRGPRX1-Galphaq in complex with BAM8-22 alone, with BAM8-22 and ML382 simultaneously as well as with a synthetic agonist compound-16. These structures reveal the agonist binding mode for MRGPRX1 and illuminate the structural requirements for positive allosteric modulation. Collectively, our findings provide a molecular understanding of the activation and allosteric modulation of the MRGPRX1 receptor, which could facilitate the structure-based design of non-opioid pain-relieving drugs.
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Ligand recognition and allosteric modulation of the human MRGPRX1 receptor.,Liu Y, Cao C, Huang XP, Gumpper RH, Rachman MM, Shih SL, Krumm BE, Zhang S, Shoichet BK, Fay JF, Roth BL Nat Chem Biol. 2023 Apr;19(4):416-422. doi: 10.1038/s41589-022-01173-6. Epub 2022 , Oct 27. PMID:36302898<ref>PMID:36302898</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 8dwc" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Transducin 3D structures|Transducin 3D structures]]
== References ==
== References ==
<references/>
<references/>

Current revision

CryoEM structure of Gq-coupled MRGPRX1 with peptide agonist BAM8-22

PDB ID 8dwc

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