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==== | ==Cryo-EM structure of human bradykinin receptor BK2R in complex Gq proteins and bradykinin== | ||
<StructureSection load='7f6h' size='340' side='right'caption='[[7f6h]]' scene=''> | <StructureSection load='7f6h' size='340' side='right'caption='[[7f6h]], [[Resolution|resolution]] 2.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<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> | <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='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> | </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> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/BKRB2_HUMAN BKRB2_HUMAN] Receptor for bradykinin. It is associated with G proteins that activate a phosphatidylinositol-calcium second messenger system.<ref>PMID:1314587</ref> <ref>PMID:1329734</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The 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<ref>PMID:35132089</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7f6h" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Transducin 3D structures|Transducin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Chen A]] | ||
[[Category: Fu Y]] | |||
[[Category: Shen J]] | |||
[[Category: Zhang D]] | |||
[[Category: Zhang H]] | |||
Revision as of 10:40, 18 January 2023
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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