8XGR
ETB-eGt complex bound to endothelin-1
8XGR の概要
| エントリーDOI | 10.2210/pdb8xgr/pdb |
| EMDBエントリー | 38330 |
| 分子名称 | Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2,eGt-alpha, Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1, Camelid antibody VHH fragment, ... (5 entities in total) |
| 機能のキーワード | signaling protein, peptide binding protein-immune system complex, peptide binding protein/immune system |
| 由来する生物種 | Bos taurus (cattle) 詳細 |
| タンパク質・核酸の鎖数 | 5 |
| 化学式量合計 | 176854.69 |
| 構造登録者 | Oshima, H.S.,Sano, F.K.,Akasaka, H.,Iwama, A.,Shihoya, W.,Nureki, O. (登録日: 2023-12-15, 公開日: 2024-04-03, 最終更新日: 2025-07-02) |
| 主引用文献 | Oshima, H.S.,Sano, F.K.,Akasaka, H.,Iwama, A.,Shihoya, W.,Nureki, O. Optimizing cryo-EM structural analysis of G i -coupling receptors via engineered G t and Nb35 application. Biochem.Biophys.Res.Commun., 693:149361-149361, 2024 Cited by 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 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. PubMed: 38128244DOI: 10.1016/j.bbrc.2023.149361 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (3.2 Å) |
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