7eib: Difference between revisions
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==== | ==Cryo-EM structure of the type 1 bradykinin receptor in complex with the des-Arg10-kallidin and an Gq protein== | ||
<StructureSection load='7eib' size='340' side='right'caption='[[7eib]]' scene=''> | <StructureSection load='7eib' size='340' side='right'caption='[[7eib]], [[Resolution|resolution]] 3.00Å' 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'>[[7eib]] is a 5 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/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7EIB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7EIB 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=7eib FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7eib OCA], [https://pdbe.org/7eib PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7eib RCSB], [https://www.ebi.ac.uk/pdbsum/7eib PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7eib ProSAT]</span></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]] 3Å</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=7eib FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7eib OCA], [https://pdbe.org/7eib PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7eib RCSB], [https://www.ebi.ac.uk/pdbsum/7eib PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7eib ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/BKRB1_HUMAN BKRB1_HUMAN] This is a receptor for bradykinin. Could be a factor in chronic pain and inflammation.<ref>PMID:8063797</ref> <ref>PMID:8660997</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Bradykinin and kallidin are endogenous kinin peptide hormones that belong to the kallikrein-kinin system and are essential to the regulation of blood pressure, inflammation, coagulation and pain control. Des-Arg(10)-kallidin, the carboxy-terminal des-Arg metabolite of kallidin, and bradykinin selectively activate two G protein-coupled receptors, type 1 and type 2 bradykinin receptors (B1R and B2R), respectively. The hyperactivation of bradykinin receptors, termed 'bradykinin storm', is associated with pulmonary edema in COVID-19 patients, suggesting that bradykinin receptors are important targets for COVID-19 intervention. Here we report two G protein-coupled complex structures of human B1R and B2R bound to des-Arg(10)-kallidin and bradykinin, respectively. Combined with functional analysis, our structures reveal the mechanism of ligand selectivity and specific activation of the bradykinin receptor. These findings also provide a framework for guiding drug design targeting bradykinin receptors for the treatment of inflammation, cardiovascular disorders and COVID-19. | |||
Molecular basis for kinin selectivity and activation of the human bradykinin receptors.,Yin YL, Ye C, Zhou F, Wang J, Yang D, Yin W, Wang MW, Xu HE, Jiang Y Nat Struct Mol Biol. 2021 Sep;28(9):755-761. doi: 10.1038/s41594-021-00645-y. , Epub 2021 Sep 9. PMID:34518695<ref>PMID:34518695</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7eib" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Transducin 3D structures|Transducin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Bos taurus]] | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Rattus norvegicus]] | ||
[[Category: Jiang Y]] | |||
[[Category: Yin Y]] | |||
Latest revision as of 09:15, 21 November 2024
Cryo-EM structure of the type 1 bradykinin receptor in complex with the des-Arg10-kallidin and an Gq proteinCryo-EM structure of the type 1 bradykinin receptor in complex with the des-Arg10-kallidin and an Gq protein
Structural highlights
FunctionBKRB1_HUMAN This is a receptor for bradykinin. Could be a factor in chronic pain and inflammation.[1] [2] Publication Abstract from PubMedBradykinin and kallidin are endogenous kinin peptide hormones that belong to the kallikrein-kinin system and are essential to the regulation of blood pressure, inflammation, coagulation and pain control. Des-Arg(10)-kallidin, the carboxy-terminal des-Arg metabolite of kallidin, and bradykinin selectively activate two G protein-coupled receptors, type 1 and type 2 bradykinin receptors (B1R and B2R), respectively. The hyperactivation of bradykinin receptors, termed 'bradykinin storm', is associated with pulmonary edema in COVID-19 patients, suggesting that bradykinin receptors are important targets for COVID-19 intervention. Here we report two G protein-coupled complex structures of human B1R and B2R bound to des-Arg(10)-kallidin and bradykinin, respectively. Combined with functional analysis, our structures reveal the mechanism of ligand selectivity and specific activation of the bradykinin receptor. These findings also provide a framework for guiding drug design targeting bradykinin receptors for the treatment of inflammation, cardiovascular disorders and COVID-19. Molecular basis for kinin selectivity and activation of the human bradykinin receptors.,Yin YL, Ye C, Zhou F, Wang J, Yang D, Yin W, Wang MW, Xu HE, Jiang Y Nat Struct Mol Biol. 2021 Sep;28(9):755-761. doi: 10.1038/s41594-021-00645-y. , Epub 2021 Sep 9. PMID:34518695[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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