6M0J
Crystal structure of SARS-CoV-2 spike receptor-binding domain bound with ACE2
Summary for 6M0J
| Entry DOI | 10.2210/pdb6m0j/pdb |
| Descriptor | Angiotensin-converting enzyme 2, Spike protein S1, ZINC ION, ... (6 entities in total) |
| Functional Keywords | spike, receptor binding, viral protein-hydrolase complex, viral protein/hydrolase |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 2 |
| Total formula weight | 97140.68 |
| Authors | |
| Primary citation | Lan, J.,Ge, J.,Yu, J.,Shan, S.,Zhou, H.,Fan, S.,Zhang, Q.,Shi, X.,Wang, Q.,Zhang, L.,Wang, X. Structure of the SARS-CoV-2 spike receptor-binding domain bound to the ACE2 receptor. Nature, 581:215-220, 2020 Cited by PubMed Abstract: A new and highly pathogenic coronavirus (severe acute respiratory syndrome coronavirus-2, SARS-CoV-2) caused an outbreak in Wuhan city, Hubei province, China, starting from December 2019 that quickly spread nationwide and to other countries around the world. Here, to better understand the initial step of infection at an atomic level, we determined the crystal structure of the receptor-binding domain (RBD) of the spike protein of SARS-CoV-2 bound to the cell receptor ACE2. The overall ACE2-binding mode of the SARS-CoV-2 RBD is nearly identical to that of the SARS-CoV RBD, which also uses ACE2 as the cell receptor. Structural analysis identified residues in the SARS-CoV-2 RBD that are essential for ACE2 binding, the majority of which either are highly conserved or share similar side chain properties with those in the SARS-CoV RBD. Such similarity in structure and sequence strongly indicate convergent evolution between the SARS-CoV-2 and SARS-CoV RBDs for improved binding to ACE2, although SARS-CoV-2 does not cluster within SARS and SARS-related coronaviruses. The epitopes of two SARS-CoV antibodies that target the RBD are also analysed for binding to the SARS-CoV-2 RBD, providing insights into the future identification of cross-reactive antibodies. PubMed: 32225176DOI: 10.1038/s41586-020-2180-5 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.45 Å) |
Structure validation
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