7DRV
Structural basis of SARS-CoV-2-closely-related bat coronavirus RaTG13 to hACE2
Summary for 7DRV
Entry DOI | 10.2210/pdb7drv/pdb |
Descriptor | Angiotensin-converting enzyme 2, Spike glycoprotein, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total) |
Functional Keywords | ratg13, rbd, sars-cov-2, ace2, viral protein, hydrolase-viral protein complex, hydrolase/viral protein |
Biological source | Homo sapiens (Human) More |
Total number of polymer chains | 4 |
Total formula weight | 190888.08 |
Authors | Liu, K.F.,Pan, X.Q.,Li, L.J.,Feng, Y.,Meng, Y.M.,Zhang, Y.F.,Wu, L.L.,Chen, Q.,Zheng, A.Q.,Song, C.L.,Jia, Y.F.,Niu, S.,Qiao, C.P.,Zhao, X.,Ma, D.L.,Ma, X.P.,Tan, S.G.,Qi, J.X.,Gao, G.F.,Wang, Q.H. (deposition date: 2020-12-29, release date: 2021-08-25, Last modification date: 2023-11-29) |
Primary citation | Liu, K.,Pan, X.,Li, L.,Yu, F.,Zheng, A.,Du, P.,Han, P.,Meng, Y.,Zhang, Y.,Wu, L.,Chen, Q.,Song, C.,Jia, Y.,Niu, S.,Lu, D.,Qiao, C.,Chen, Z.,Ma, D.,Ma, X.,Tan, S.,Zhao, X.,Qi, J.,Gao, G.F.,Wang, Q. Binding and molecular basis of the bat coronavirus RaTG13 virus to ACE2 in humans and other species. Cell, 184:3438-3451.e10, 2021 Cited by PubMed Abstract: Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has been spreading worldwide, causing a global pandemic. Bat-origin RaTG13 is currently the most phylogenetically related virus. Here we obtained the complex structure of the RaTG13 receptor binding domain (RBD) with human ACE2 (hACE2) and evaluated binding of RaTG13 RBD to 24 additional ACE2 orthologs. By substituting residues in the RaTG13 RBD with their counterparts in the SARS-CoV-2 RBD, we found that residue 501, the major position found in variants of concern (VOCs) 501Y.V1/V2/V3, plays a key role in determining the potential host range of RaTG13. We also found that SARS-CoV-2 could induce strong cross-reactive antibodies to RaTG13 and identified a SARS-CoV-2 monoclonal antibody (mAb), CB6, that could cross-neutralize RaTG13 pseudovirus. These results elucidate the receptor binding and host adaption mechanisms of RaTG13 and emphasize the importance of continuous surveillance of coronaviruses (CoVs) carried by animal reservoirs to prevent another spillover of CoVs. PubMed: 34139177DOI: 10.1016/j.cell.2021.05.031 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.09 Å) |
Structure validation
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