6LZG
Structure of novel coronavirus spike receptor-binding domain complexed with its receptor ACE2
Summary for 6LZG
| Entry DOI | 10.2210/pdb6lzg/pdb |
| Descriptor | Angiotensin-converting enzyme 2, Spike protein S1, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total) |
| Functional Keywords | novel coronavirus, spike protein, receptor, viral protein |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 2 |
| Total formula weight | 93502.21 |
| Authors | Wang, Q.H.,Song, H.,Qi, J.X. (deposition date: 2020-02-19, release date: 2020-03-18, Last modification date: 2024-11-06) |
| Primary citation | Wang, Q.,Zhang, Y.,Wu, L.,Niu, S.,Song, C.,Zhang, Z.,Lu, G.,Qiao, C.,Hu, Y.,Yuen, K.Y.,Wang, Q.,Zhou, H.,Yan, J.,Qi, J. Structural and Functional Basis of SARS-CoV-2 Entry by Using Human ACE2. Cell, 181:894-904.e9, 2020 Cited by PubMed Abstract: The recent emergence of a novel coronavirus (SARS-CoV-2) in China has caused significant public health concerns. Recently, ACE2 was reported as an entry receptor for SARS-CoV-2. In this study, we present the crystal structure of the C-terminal domain of SARS-CoV-2 (SARS-CoV-2-CTD) spike (S) protein in complex with human ACE2 (hACE2), which reveals a hACE2-binding mode similar overall to that observed for SARS-CoV. However, atomic details at the binding interface demonstrate that key residue substitutions in SARS-CoV-2-CTD slightly strengthen the interaction and lead to higher affinity for receptor binding than SARS-RBD. Additionally, a panel of murine monoclonal antibodies (mAbs) and polyclonal antibodies (pAbs) against SARS-CoV-S1/receptor-binding domain (RBD) were unable to interact with the SARS-CoV-2 S protein, indicating notable differences in antigenicity between SARS-CoV and SARS-CoV-2. These findings shed light on the viral pathogenesis and provide important structural information regarding development of therapeutic countermeasures against the emerging virus. PubMed: 32275855DOI: 10.1016/j.cell.2020.03.045 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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