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| Title | Optimizing cryo-EM structural analysis of G-coupling receptors via engineered G and Nb35 application. |
|---|---|
| Journal, issue, pages | Biochem Biophys Res Commun, Vol. 693, Page 149361, Year 2024 |
| Publish date | Jan 22, 2024 |
 Authors | Hidetaka S Oshima / Fumiya K Sano / Hiroaki Akasaka / Aika Iwama / Wataru Shihoya / Osamu Nureki /  |
| PubMed Abstract | 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 ...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 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 complexes remain both challenging and resource-intensive. By employing eGα, which exhibits binding affinity to modified nanobody Nb35, the cryo-EM structure of Rhodopsin-eGα complex was previously reported. Using this modified G protein, we determined the structure of the ET-eG complex bound to the modified Nb35. The determined structure of ET receptor was the same as the previously reported ET-G complex, and the resulting dataset demonstrated significantly improved anisotropy. This modified G protein will be utilized for the structural determination of other GPCR-G complexes. |
 External links | Biochem Biophys Res Commun / PubMed:38128244 |
| Methods | EM (single particle) |
| Resolution | 3.2 Å |
| Structure data | EMDB-38330, PDB-8xgr: |
| Source |
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 Keywords | PEPTIDE BINDING PROTEIN/IMMUNE SYSTEM /  SIGNALING PROTEIN / PEPTIDE BINDING PROTEIN-IMMUNE SYSTEM complex |
