8YF2
Cryo-EM structure of SARS-CoV-2 prototype RBD in complex with raccoon dog ACE2 (local refinement)
8YF2 の概要
| エントリーDOI | 10.2210/pdb8yf2/pdb |
| EMDBエントリー | 39208 |
| 分子名称 | Spike protein S1, Angiotensin-converting enzyme, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total) |
| 機能のキーワード | sars-cov-2, rototype rbd, raccoon dog, ace2, viral protein-hydrolase complex, viral protein/hydrolase |
| 由来する生物種 | Severe acute respiratory syndrome coronavirus 2 詳細 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 98535.53 |
| 構造登録者 | |
| 主引用文献 | Luo, C.,Li, L.,Gu, Y.,Zhang, H.,Xu, Z.,Sun, J.,Shi, K.,Ma, S.,Tian, W.X.,Liu, K.,Gao, G.F. Receptor binding and structural basis of raccoon dog ACE2 binding to SARS-CoV-2 prototype and its variants. Plos Pathog., 20:e1012713-e1012713, 2024 Cited by PubMed Abstract: Raccoon dog was proposed as a potential host of SARS-CoV-2, but no evidence support such a notion. In our study, we investigated the binding affinities of raccoon dog ACE2 (rdACE2) to the spike (S) protein receptor binding domain (RBD) of SARS-CoV-2 prototype (PT) and its variants. It revealed that the binding affinities of RBD from SARS-CoV-2 variants were generally lower than that of the PT RBD. Through structural and functional analyses, we found amino acids H34 and M82 play pivotal roles in maintaining the binding affinity of ACE2 to different SARS-CoV-2 sub-variants. These results suggest that raccoon dogs exhibit lower susceptibility to SARS-CoV-2 compared to those animal species with a high prevalence of SARS-CoV-2 transmission. PubMed: 39637248DOI: 10.1371/journal.ppat.1012713 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (2.64 Å) |
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