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7MJG

Cryo-EM structure of the SARS-CoV-2 N501Y mutant spike protein ectodomain

7MJG の概要
エントリーDOI10.2210/pdb7mjg/pdb
EMDBエントリー23872
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 (3 entities in total)
機能のキーワードsars-cov-2, glycoprotein, fusion protein, 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440377.71
構造登録者
主引用文献Zhu, X.,Mannar, D.,Srivastava, S.S.,Berezuk, A.M.,Demers, J.P.,Saville, J.W.,Leopold, K.,Li, W.,Dimitrov, D.S.,Tuttle, K.S.,Zhou, S.,Chittori, S.,Subramaniam, S.
Cryo-electron microscopy structures of the N501Y SARS-CoV-2 spike protein in complex with ACE2 and 2 potent neutralizing antibodies.
Plos Biol., 19:e3001237-e3001237, 2021
Cited by
PubMed Abstract: The recently reported "UK variant" (B.1.1.7) of SARS-CoV-2 is thought to be more infectious than previously circulating strains as a result of several changes, including the N501Y mutation. We present a 2.9-Å resolution cryo-electron microscopy (cryo-EM) structure of the complex between the ACE2 receptor and N501Y spike protein ectodomains that shows Y501 inserted into a cavity at the binding interface near Y41 of ACE2. This additional interaction provides a structural explanation for the increased ACE2 affinity of the N501Y mutant, and likely contributes to its increased infectivity. However, this mutation does not result in large structural changes, enabling important neutralization epitopes to be retained in the spike receptor binding domain. We confirmed this through biophysical assays and by determining cryo-EM structures of spike protein ectodomains bound to 2 representative potent neutralizing antibody fragments.
PubMed: 33914735
DOI: 10.1371/journal.pbio.3001237
主引用文献が同じPDBエントリー
実験手法
ELECTRON MICROSCOPY (2.81 Å)
構造検証レポート
Validation report summary of 7mjg
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2025-12-31に公開中

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