8iy5: Difference between revisions
New page: '''Unreleased structure''' The entry 8iy5 is ON HOLD Authors: Sano, F.K., Akasaka, H., Shihoya, W., Nureki, O. Description: ETB-Gi complex bound to endothelin-1 [[Category: Unreleased ... |
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The | ==ETB-Gi complex bound to endothelin-1== | ||
<StructureSection load='8iy5' size='340' side='right'caption='[[8iy5]], [[Resolution|resolution]] 2.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8iy5]] 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], [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Rattus_rattus Rattus rattus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8IY5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8IY5 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.8Å</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=8iy5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8iy5 OCA], [https://pdbe.org/8iy5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8iy5 RCSB], [https://www.ebi.ac.uk/pdbsum/8iy5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8iy5 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The endothelin ET(B) receptor is a promiscuous G-protein coupled receptor that is activated by vasoactive peptide endothelins. ET(B) signaling induces reactive astrocytes in the brain and vasorelaxation in vascular smooth muscle. Consequently, ET(B) agonists are expected to be drugs for neuroprotection and improved anti-tumor drug delivery. Here, we report the cryo-electron microscopy structure of the endothelin-1-ET(B)-G(i) complex at 2.8 A resolution, with complex assembly stabilized by a newly established method. Comparisons with the inactive ET(B) receptor structures revealed how endothelin-1 activates the ET(B) receptor. The NPxxY motif, essential for G-protein activation, is not conserved in ET(B), resulting in a unique structural change upon G-protein activation. Compared with other GPCR-G-protein complexes, ET(B) binds G(i) in the shallowest position, further expanding the diversity of G-protein binding modes. This structural information will facilitate the elucidation of G-protein activation and the rational design of ET(B) agonists. | |||
Cryo-EM structure of the endothelin-1-ET(B)-G(i) complex.,Sano FK, Akasaka H, Shihoya W, Nureki O Elife. 2023 Apr 25;12:e85821. doi: 10.7554/eLife.85821. PMID:37096326<ref>PMID:37096326</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 8iy5" style="background-color:#fffaf0;"></div> | ||
[[Category: Akasaka | == References == | ||
[[Category: Sano | <references/> | ||
[[Category: Shihoya | __TOC__ | ||
</StructureSection> | |||
[[Category: Bos taurus]] | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Mus musculus]] | |||
[[Category: Rattus rattus]] | |||
[[Category: Akasaka H]] | |||
[[Category: Nureki O]] | |||
[[Category: Sano FK]] | |||
[[Category: Shihoya W]] | |||
Latest revision as of 12:44, 17 October 2024
ETB-Gi complex bound to endothelin-1ETB-Gi complex bound to endothelin-1
Structural highlights
Publication Abstract from PubMedThe endothelin ET(B) receptor is a promiscuous G-protein coupled receptor that is activated by vasoactive peptide endothelins. ET(B) signaling induces reactive astrocytes in the brain and vasorelaxation in vascular smooth muscle. Consequently, ET(B) agonists are expected to be drugs for neuroprotection and improved anti-tumor drug delivery. Here, we report the cryo-electron microscopy structure of the endothelin-1-ET(B)-G(i) complex at 2.8 A resolution, with complex assembly stabilized by a newly established method. Comparisons with the inactive ET(B) receptor structures revealed how endothelin-1 activates the ET(B) receptor. The NPxxY motif, essential for G-protein activation, is not conserved in ET(B), resulting in a unique structural change upon G-protein activation. Compared with other GPCR-G-protein complexes, ET(B) binds G(i) in the shallowest position, further expanding the diversity of G-protein binding modes. This structural information will facilitate the elucidation of G-protein activation and the rational design of ET(B) agonists. Cryo-EM structure of the endothelin-1-ET(B)-G(i) complex.,Sano FK, Akasaka H, Shihoya W, Nureki O Elife. 2023 Apr 25;12:e85821. doi: 10.7554/eLife.85821. PMID:37096326[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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