7SXU
Cryo-EM structure of the SARS-CoV-2 D614G,N501Y,E484K mutant spike protein ectodomain
Summary for 7SXU
| Entry DOI | 10.2210/pdb7sxu/pdb |
| EMDB information | 25506 |
| Descriptor | 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) |
| Functional Keywords | sars-cov-2, glycoprotein, fusion protein, viral protein |
| Biological source | Severe acute respiratory syndrome coronavirus 2 (2019-nCoV, SARS-CoV-2) |
| Total number of polymer chains | 3 |
| Total formula weight | 440203.80 |
| Authors | Zhu, X.,Mannar, D.,Saville, J.W.,Srivastava, S.S.,Berezuk, A.M.,Zhou, S.,Tuttle, K.S.,Kim, A.,Li, W.,Dimitrov, D.S.,Subramaniam, S. (deposition date: 2021-11-24, release date: 2021-12-29, Last modification date: 2024-11-13) |
| Primary citation | Mannar, D.,Saville, J.W.,Zhu, X.,Srivastava, S.S.,Berezuk, A.M.,Zhou, S.,Tuttle, K.S.,Kim, A.,Li, W.,Dimitrov, D.S.,Subramaniam, S. Structural analysis of receptor binding domain mutations in SARS-CoV-2 variants of concern that modulate ACE2 and antibody binding. Cell Rep, 37:110156-110156, 2021 Cited by PubMed Abstract: The recently emerged severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) Beta (B.1.351) and Gamma (P.1) variants of concern (VoCs) include a key mutation (N501Y) found in the Alpha (B.1.1.7) variant that enhances affinity of the spike protein for its receptor, angiotensin-converting enzyme 2 (ACE2). Additional mutations are found in these variants at residues 417 and 484 that appear to promote antibody evasion. In contrast, the Epsilon variants (B.1.427/429) lack the N501Y mutation yet exhibit antibody evasion. We have engineered spike proteins to express these receptor binding domain (RBD) VoC mutations either in isolation or in different combinations and analyze the effects using biochemical assays and cryoelectron microscopy (cryo-EM) structural analyses. Overall, our findings suggest that the emergence of new SARS-CoV-2 variant spikes can be rationalized as the result of mutations that confer increased ACE2 affinity, increased antibody evasion, or both, providing a framework to dissect the molecular factors that drive VoC evolution. PubMed: 34914928DOI: 10.1016/j.celrep.2021.110156 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3 Å) |
Structure validation
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