7f6h: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7f6h]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7F6H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7F6H FirstGlance]. <br> | <table><tr><td colspan='2'>[[7f6h]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7F6H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7F6H FirstGlance]. <br> | ||
</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> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.9Å</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=7f6h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7f6h OCA], [https://pdbe.org/7f6h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7f6h RCSB], [https://www.ebi.ac.uk/pdbsum/7f6h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7f6h ProSAT]</span></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=7f6h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7f6h OCA], [https://pdbe.org/7f6h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7f6h RCSB], [https://www.ebi.ac.uk/pdbsum/7f6h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7f6h ProSAT]</span></td></tr> | ||
</table> | </table> | ||
Latest revision as of 14:01, 23 October 2024
Cryo-EM structure of human bradykinin receptor BK2R in complex Gq proteins and bradykininCryo-EM structure of human bradykinin receptor BK2R in complex Gq proteins and bradykinin
Structural highlights
FunctionBKRB2_HUMAN Receptor for bradykinin. It is associated with G proteins that activate a phosphatidylinositol-calcium second messenger system.[1] [2] Publication Abstract from PubMedThe type 2 bradykinin receptor (B2R) is a G protein-coupled receptor (GPCR) in the cardiovascular system, and the dysfunction of B2R leads to inflammation, hereditary angioedema, and pain. Bradykinin and kallidin are both endogenous peptide agonists of B2R, acting as vasodilators to protect the cardiovascular system. Here we determine two cryo-electron microscopy (cryo-EM) structures of human B2R-G(q) in complex with bradykinin and kallidin at 3.0 A and 2.9 A resolution, respectively. The ligand-binding pocket accommodates S-shaped peptides, with aspartic acids and glutamates as an anion trap. The phenylalanines at the tail of the peptides induce significant conformational changes in the toggle switch W283(6.48), the conserved PIF, DRY, and NPxxY motifs, for the B2R activation. This further induces the extensive interactions of the intracellular loops ICL2/3 and helix 8 with G(q) proteins. Our structures elucidate the molecular mechanisms for the ligand binding, receptor activation, and G(q) proteins coupling of B2R. Cryo-EM structures of human bradykinin receptor-G(q) proteins complexes.,Shen J, Zhang D, Fu Y, Chen A, Yang X, Zhang H Nat Commun. 2022 Feb 7;13(1):714. doi: 10.1038/s41467-022-28399-1. PMID:35132089[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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