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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DOI10.2210/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
Li, L.J.,Luo, C.L.,Qi, J.X.,Gao, G.F. (登録日: 2024-02-23, 公開日: 2024-10-23, 最終更新日: 2025-04-30)
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: 39637248
DOI: 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)
構造検証レポート
Validation report summary of 8yf2
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-02-04に公開中

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