8XYE
Crystal structure of SARS-CoV-2 BA.4 RBD and human ACE2
Summary for 8XYE
| Entry DOI | 10.2210/pdb8xye/pdb |
| Descriptor | Processed angiotensin-converting enzyme 2, Spike protein S1, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total) |
| Functional Keywords | sars-cov-2 ba.4, human ace2, viral protein/hydrolase, viral protein-hydrolase complex |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 4 |
| Total formula weight | 186113.47 |
| Authors | Lan, J.,Wang, C.H. (deposition date: 2024-01-19, release date: 2025-01-22, Last modification date: 2025-04-16) |
| Primary citation | Wang, C.,Zhang, Y.,Yang, C.,Ren, W.,Qiu, C.,Fan, S.,Ding, Q.,Lan, J. Receptor binding mechanism and immune evasion capacity of SARS-CoV-2 BQ.1.1 lineage. Virology, 600:110241-110241, 2024 Cited by PubMed Abstract: The global spread of COVID-19 remains a significant threat to human health. The SARS-CoV-2 BQ.1.1 lineage, including BA.5.2, BF.7, BQ.1 and BQ.1.1, caused a new soaring of infection cases due to rapid transmission. However, the receptor binding mechanism and immune evasion capacity of these variants need to be explored further. Our study found that while the BA.5.2, BF.7 and BQ.1.1 variants pseudovirus had similar cell entry efficiency, the BF.7 and BQ.1.1 RBD bound to human ACE2 (hACE2) with a slightly stronger affinity than the BA.5.2 RBD. Structural analysis revealed R346T, K444T, and N460K mutations altered RBD-hACE2 binding interface details and surface electrostatic potential of BQ.1.1 RBD. Serum neutralization tests showed BQ.1.1 variant had stronger immune evasion capacity than BA.5.2 and BF.7 variants. Our findings illustrated the receptor binding mechanism and serological neutralization activity of the BA.5.2, BF.7 and BQ.1.1 variants, which verified the necessity for further antibody therapy optimization and vaccination development. PubMed: 39270455DOI: 10.1016/j.virol.2024.110241 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.32 Å) |
Structure validation
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