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7NEG

Crystal structure of the N501Y mutant receptor binding domain of SARS-CoV-2 Spike glycoprotein in complex with COVOX-269 Fab

7NEG の概要
エントリーDOI10.2210/pdb7neg/pdb
分子名称Antibody COVOX-269 Fab heavy chain, Antibody COVOX-269 Fab light chain, Surface glycoprotein, ... (7 entities in total)
機能のキーワードsars-cov-2 b.1.1.7 variant, n501y mutation, antibody, receptor-binding-domain, spike, neutralisation, viral protein/immune system, viral protein-immune system complex
由来する生物種Homo sapiens (Human)
詳細
タンパク質・核酸の鎖数3
化学式量合計71838.14
構造登録者
Zhou, D.,Ren, J.,Stuart, D. (登録日: 2021-02-04, 公開日: 2021-03-03, 最終更新日: 2024-01-31)
主引用文献Supasa, P.,Zhou, D.,Dejnirattisai, W.,Liu, C.,Mentzer, A.J.,Ginn, H.M.,Zhao, Y.,Duyvesteyn, H.M.E.,Nutalai, R.,Tuekprakhon, A.,Wang, B.,Paesen, G.C.,Slon-Campos, J.,Lopez-Camacho, C.,Hallis, B.,Coombes, N.,Bewley, K.R.,Charlton, S.,Walter, T.S.,Barnes, E.,Dunachie, S.J.,Skelly, D.,Lumley, S.F.,Baker, N.,Shaik, I.,Humphries, H.E.,Godwin, K.,Gent, N.,Sienkiewicz, A.,Dold, C.,Levin, R.,Dong, T.,Pollard, A.J.,Knight, J.C.,Klenerman, P.,Crook, D.,Lambe, T.,Clutterbuck, E.,Bibi, S.,Flaxman, A.,Bittaye, M.,Belij-Rammerstorfer, S.,Gilbert, S.,Hall, D.R.,Williams, M.A.,Paterson, N.G.,James, W.,Carroll, M.W.,Fry, E.E.,Mongkolsapaya, J.,Ren, J.,Stuart, D.I.,Screaton, G.R.
Reduced neutralization of SARS-CoV-2 B.1.1.7 variant by convalescent and vaccine sera.
Cell, 184:2201-, 2021
Cited by
PubMed Abstract: SARS-CoV-2 has caused over 2 million deaths in little over a year. Vaccines are being deployed at scale, aiming to generate responses against the virus spike. The scale of the pandemic and error-prone virus replication is leading to the appearance of mutant viruses and potentially escape from antibody responses. Variant B.1.1.7, now dominant in the UK, with increased transmission, harbors 9 amino acid changes in the spike, including N501Y in the ACE2 interacting surface. We examine the ability of B.1.1.7 to evade antibody responses elicited by natural SARS-CoV-2 infection or vaccination. We map the impact of N501Y by structure/function analysis of a large panel of well-characterized monoclonal antibodies. B.1.1.7 is harder to neutralize than parental virus, compromising neutralization by some members of a major class of public antibodies through light-chain contacts with residue 501. However, widespread escape from monoclonal antibodies or antibody responses generated by natural infection or vaccination was not observed.
PubMed: 33743891
DOI: 10.1016/j.cell.2021.02.033
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.19 Å)
構造検証レポート
Validation report summary of 7neg
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2024-10-30に公開中

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