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TitleOptimizing cryo-EM structural analysis of G-coupling receptors via engineered G and Nb35 application.
Journal, issue, pagesBiochem Biophys Res Commun, Vol. 693, Page 149361, Year 2024
Publish dateJan 22, 2024
AuthorsHidetaka S Oshima / Fumiya K Sano / Hiroaki Akasaka / Aika Iwama / Wataru Shihoya / Osamu Nureki /
PubMed AbstractCryo-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 linksBiochem Biophys Res Commun / PubMed:38128244
MethodsEM (single particle)
Resolution3.2 Å
Structure data

38330

8xgr

EMDB-38330, PDB-8xgr:
ETB-eGt complex bound to endothelin-1
Method: EM (single particle) / Resolution: 3.2 Å

Source
  • homo sapiens (human)
  • bos taurus (domestic cattle)
  • rattus rattus (black rat)
  • lama glama (llama)
KeywordsPEPTIDE BINDING PROTEIN/IMMUNE SYSTEM / SIGNALING PROTEIN / PEPTIDE BINDING PROTEIN-IMMUNE SYSTEM complex

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