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7N1Y

Structural basis for enhanced infectivity and immune evasion of SARS-CoV-2 variants

Summary for 7N1Y
Entry DOI10.2210/pdb7n1y/pdb
EMDB information24127
DescriptorSpike 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)
Functional Keywordsviral protein
Biological sourceSevere acute respiratory syndrome coronavirus 2 (2019-nCoV, SARS-CoV-2)
Total number of polymer chains3
Total formula weight452205.45
Authors
Zhang, J.,Cai, Y.F.,Xiao, T.S.,Rawson, S.,Peng, H.Q.,Sterling, S.M.,Walsh Jr, R.M.,Volloch, S.R.,Chen, B. (deposition date: 2021-05-28, release date: 2021-07-07, Last modification date: 2024-11-06)
Primary citationCai, Y.,Zhang, J.,Xiao, T.,Lavine, C.L.,Rawson, S.,Peng, H.,Zhu, H.,Anand, K.,Tong, P.,Gautam, A.,Lu, S.,Sterling, S.M.,Walsh Jr., R.M.,Rits-Volloch, S.,Lu, J.,Wesemann, D.R.,Yang, W.,Seaman, M.S.,Chen, B.
Structural basis for enhanced infectivity and immune evasion of SARS-CoV-2 variants.
Science, 373:642-648, 2021
Cited by
PubMed Abstract: Several fast-spreading variants of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) have become the dominant circulating strains in the COVID-19 pandemic. We report here cryo-electron microscopy structures of the full-length spike (S) trimers of the B.1.1.7 and B.1.351 variants, as well as their biochemical and antigenic properties. Amino acid substitutions in the B.1.1.7 protein increase both the accessibility of its receptor binding domain and the binding affinity for receptor angiotensin-converting enzyme 2 (ACE2). The enhanced receptor engagement may account for the increased transmissibility. The B.1.351 variant has evolved to reshape antigenic surfaces of the major neutralizing sites on the S protein, making it resistant to some potent neutralizing antibodies. These findings provide structural details on how SARS-CoV-2 has evolved to enhance viral fitness and immune evasion.
PubMed: 34168070
DOI: 10.1126/science.abi9745
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (4.3 Å)
Structure validation

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