8xgr: Difference between revisions
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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=8xgr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8xgr OCA], [https://pdbe.org/8xgr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8xgr RCSB], [https://www.ebi.ac.uk/pdbsum/8xgr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8xgr 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=8xgr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8xgr OCA], [https://pdbe.org/8xgr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8xgr RCSB], [https://www.ebi.ac.uk/pdbsum/8xgr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8xgr ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | |||
Cryo-EM single particle analysis has recently facilitated the high-resolution structural determination of numerous GPCR-G complexes. Diverse methodologies have been devised with this trend, and in the case of GPCR-G(i) complexes, scFv16, an antibody that recognizes the intricate interface of the complex, has been mainly implemented to stabilize the complex. However, owing to their flexibility and heterogeneity, structural determinations of GPCR-G(i) complexes remain both challenging and resource-intensive. By employing eGalpha(t), which exhibits binding affinity to modified nanobody Nb35, the cryo-EM structure of Rhodopsin-eGalpha(t) complex was previously reported. Using this modified G protein, we determined the structure of the ET(B)-eG(t) complex bound to the modified Nb35. The determined structure of ET(B) receptor was the same as the previously reported ET(B)-G(i) complex, and the resulting dataset demonstrated significantly improved anisotropy. This modified G protein will be utilized for the structural determination of other GPCR-G(i) complexes. | |||
Optimizing cryo-EM structural analysis of G(i)-coupling receptors via engineered G(t) and Nb35 application.,Oshima HS, Sano FK, Akasaka H, Iwama A, Shihoya W, Nureki O Biochem Biophys Res Commun. 2024 Jan 22;693:149361. doi: , 10.1016/j.bbrc.2023.149361. Epub 2023 Dec 7. PMID:38128244<ref>PMID:38128244</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 8xgr" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Latest revision as of 13:04, 9 October 2024
ETB-eGt complex bound to endothelin-1ETB-eGt complex bound to endothelin-1
Structural highlights
Publication Abstract from PubMedCryo-EM single particle analysis has recently facilitated the high-resolution structural determination of numerous GPCR-G complexes. Diverse methodologies have been devised with this trend, and in the case of GPCR-G(i) complexes, scFv16, an antibody that recognizes the intricate interface of the complex, has been mainly implemented to stabilize the complex. However, owing to their flexibility and heterogeneity, structural determinations of GPCR-G(i) complexes remain both challenging and resource-intensive. By employing eGalpha(t), which exhibits binding affinity to modified nanobody Nb35, the cryo-EM structure of Rhodopsin-eGalpha(t) complex was previously reported. Using this modified G protein, we determined the structure of the ET(B)-eG(t) complex bound to the modified Nb35. The determined structure of ET(B) receptor was the same as the previously reported ET(B)-G(i) complex, and the resulting dataset demonstrated significantly improved anisotropy. This modified G protein will be utilized for the structural determination of other GPCR-G(i) complexes. Optimizing cryo-EM structural analysis of G(i)-coupling receptors via engineered G(t) and Nb35 application.,Oshima HS, Sano FK, Akasaka H, Iwama A, Shihoya W, Nureki O Biochem Biophys Res Commun. 2024 Jan 22;693:149361. doi: , 10.1016/j.bbrc.2023.149361. Epub 2023 Dec 7. PMID:38128244[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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