7SBR
One RBD-up 2 of pre-fusion SARS-CoV-2 Kappa variant spike protein
7SBR の概要
エントリーDOI | 10.2210/pdb7sbr/pdb |
EMDBエントリー | 24986 |
分子名称 | Spike glycoprotein, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total) |
機能のキーワード | viral protein |
由来する生物種 | Severe acute respiratory syndrome coronavirus 2 (2019-nCoV, SARS-CoV-2) |
タンパク質・核酸の鎖数 | 3 |
化学式量合計 | 456422.86 |
構造登録者 | Zhang, J.,Xiao, T.S.,Cai, Y.F.,Peng, H.Q.,Volloch, S.R.,Chen, B. (登録日: 2021-09-25, 公開日: 2021-11-03, 最終更新日: 2024-10-23) |
主引用文献 | Zhang, J.,Xiao, T.,Cai, Y.,Lavine, C.L.,Peng, H.,Zhu, H.,Anand, K.,Tong, P.,Gautam, A.,Mayer, M.L.,Walsh Jr., R.M.,Rits-Volloch, S.,Wesemann, D.R.,Yang, W.,Seaman, M.S.,Lu, J.,Chen, B. Membrane fusion and immune evasion by the spike protein of SARS-CoV-2 Delta variant. Science, 374:1353-1360, 2021 Cited by PubMed Abstract: The Delta variant of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has outcompeted previously prevalent variants and become a dominant strain worldwide. We report the structure, function, and antigenicity of its full-length spike (S) trimer as well as those of the Gamma and Kappa variants, and compare their characteristics with the G614, Alpha, and Beta variants. Delta S can fuse membranes more efficiently at low levels of cellular receptor angiotensin converting enzyme 2 (ACE2), and its pseudotyped viruses infect target cells substantially faster than the other five variants, possibly accounting for its heightened transmissibility. Each variant shows different rearrangement of the antigenic surface of the amino-terminal domain of the S protein but only makes produces changes in the receptor binding domain (RBD), making the RBD a better target for therapeutic antibodies. PubMed: 34698504DOI: 10.1126/science.abl9463 主引用文献が同じPDBエントリー |
実験手法 | ELECTRON MICROSCOPY (4.3 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード
