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- W4387461102 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 the case of GPCR-Gi 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-Gi complexes remain both challenging and resource-intensive. By employing eGαt, which exhibits binding affinity to modified nanobody Nb35, the cryo-EM structure of Rhodopsin-eGαt complex was previously reported. Using this modified G protein, we determined the structure of the ETB-eGt complex bound to the modified Nb35. The determined structure of ETB receptor was the same as the previously reported ETB-Gi complex, and the resulting dataset demonstrated significantly improved anisotropy. This modified G protein will be utilized for the structural determination of other GPCR-Gi complexes." @default.
- W4387461102 created "2023-10-10" @default.
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- W4387461102 date "2023-10-07" @default.
- W4387461102 modified "2023-10-11" @default.
- W4387461102 title "Optimizing Cryo-EM Structural Analysis of Gi-coupling Receptors via Engineered Gt and Nb35 Application" @default.
- W4387461102 doi "https://doi.org/10.1101/2023.10.07.561347" @default.
- W4387461102 hasPublicationYear "2023" @default.
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