7EKC
Structure of SARS-CoV-2 Gamma variant spike receptor-binding domain complexed with human ACE2
Summary for 7EKC
| Entry DOI | 10.2210/pdb7ekc/pdb |
| Descriptor | Angiotensin-converting enzyme 2, Spike protein S1, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total) |
| Functional Keywords | sars-cov-2, spike, rbd, 501y.v3, ace2, viral protein, hydrolase-viral protein complex, hydrolase/viral protein |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 2 |
| Total formula weight | 97550.69 |
| Authors | Han, P.C.,Su, C.,Zhang, Y.F.,Qi, J.X.,Gao, G.F. (deposition date: 2021-04-05, release date: 2021-11-03, Last modification date: 2024-11-06) |
| Primary citation | Han, P.,Su, C.,Zhang, Y.,Bai, C.,Zheng, A.,Qiao, C.,Wang, Q.,Niu, S.,Chen, Q.,Zhang, Y.,Li, W.,Liao, H.,Li, J.,Zhang, Z.,Cho, H.,Yang, M.,Rong, X.,Hu, Y.,Huang, N.,Yan, J.,Wang, Q.,Zhao, X.,Gao, G.F.,Qi, J. Molecular insights into receptor binding of recent emerging SARS-CoV-2 variants. Nat Commun, 12:6103-6103, 2021 Cited by PubMed Abstract: Multiple SARS-CoV-2 variants of concern (VOCs) have been emerging and some have been linked to an increase in case numbers globally. However, there is yet a lack of understanding of the molecular basis for the interactions between the human ACE2 (hACE2) receptor and these VOCs. Here we examined several VOCs including Alpha, Beta, and Gamma, and demonstrate that five variants receptor-binding domain (RBD) increased binding affinity for hACE2, and four variants pseudoviruses increased entry into susceptible cells. Crystal structures of hACE2-RBD complexes help identify the key residues facilitating changes in hACE2 binding affinity. Additionally, soluble hACE2 protein efficiently prevent most of the variants pseudoviruses. Our findings provide important molecular information and may help the development of novel therapeutic and prophylactic agents targeting these emerging mutants. PubMed: 34671049DOI: 10.1038/s41467-021-26401-w PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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