7t6v

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==Structure of the human FPR2-Gi complex with fMLFII==
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<StructureSection load='7t6v' size='340' side='right'caption='[[7t6v]]' scene=''>
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<StructureSection load='7t6v' size='340' side='right'caption='[[7t6v]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br>
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<table><tr><td colspan='2'>[[7t6v]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus], [https://en.wikipedia.org/wiki/Homo Homo], [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Rattus Rattus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7T6V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7T6V 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=7t6v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7t6v OCA], [https://pdbe.org/7t6v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7t6v RCSB], [https://www.ebi.ac.uk/pdbsum/7t6v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7t6v ProSAT]</span></td></tr>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FME:N-FORMYLMETHIONINE'>FME</scene>, <scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</scene></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=7t6v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7t6v OCA], [https://pdbe.org/7t6v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7t6v RCSB], [https://www.ebi.ac.uk/pdbsum/7t6v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7t6v ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/FPR2_HUMAN FPR2_HUMAN] Low affinity receptor for N-formyl-methionyl peptides, which are powerful neutrophil chemotactic factors (PubMed:1374236). Binding of FMLP to the receptor causes activation of neutrophils (PubMed:1374236). This response is mediated via a G-protein that activates a phosphatidylinositol-calcium second messenger system (PubMed:1374236). The activation of LXA4R could result in an anti-inflammatory outcome counteracting the actions of proinflammatory signals such as LTB4 (leukotriene B4) (PubMed:9547339). Receptor for the chemokine-like protein FAM19A5, mediating FAM19A5-stimulated macrophage chemotaxis and the inhibitory effect on TNFSF11/RANKL-induced osteoclast differentiation (By similarity).[UniProtKB:O88536]<ref>PMID:1374236</ref> <ref>PMID:9547339</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The formylpeptide receptors (FPRs) mediate pattern recognition of formylated peptides derived from invading pathogens or mitochondria from dead host cells. They can also sense other structurally distinct native peptides and even lipid mediators to either promote or resolve inflammation. Pharmacological targeting of FPRs represents a novel therapeutic approach in treating inflammatory diseases. However, the molecular mechanisms underlying FPR ligand recognition are elusive. We report cryo-EM structures of Gi-coupled FPR1 and FPR2 bound to a formylpeptide and Gi-coupled FPR2 bound to two synthetic peptide and small-molecule agonists. Together with mutagenesis data, our structures reveal the molecular mechanism of formylpeptide recognition by FPRs and structural variations of FPR1 and FPR2 leading to their different ligand preferences. Structural analysis also suggests that diverse FPR agonists sample a conserved activation chamber at the bottom of ligand-binding pockets to activate FPRs. Our results provide a basis for rational drug design on FPRs.
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Molecular recognition of formylpeptides and diverse agonists by the formylpeptide receptors FPR1 and FPR2.,Zhuang Y, Wang L, Guo J, Sun D, Wang Y, Liu W, Xu HE, Zhang C Nat Commun. 2022 Feb 25;13(1):1054. doi: 10.1038/s41467-022-28586-0. PMID:35217703<ref>PMID:35217703</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 7t6v" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Transducin 3D structures|Transducin 3D structures]]
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bos taurus]]
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[[Category: Homo]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Z-disk]]
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[[Category: Rattus]]
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[[Category: Zhuang YW]]

Revision as of 19:32, 19 October 2022

Structure of the human FPR2-Gi complex with fMLFII

PDB ID 7t6v

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