8VQR
Crystal structure of chimeric SARS-CoV-2 RBD complexed with chimeric raccoon dog ACE2
Summary for 8VQR
| Entry DOI | 10.2210/pdb8vqr/pdb |
| Descriptor | Angiotensin-converting enzyme,Processed angiotensin-converting enzyme 2, CHLORIDE ION, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (13 entities in total) |
| Functional Keywords | sars2, cell invasion, hydrolase-viral protein complex, hydrolase, hydrolase/viral protein |
| Biological source | Nyctereutes procyonoides (raccoon dog) More |
| Total number of polymer chains | 4 |
| Total formula weight | 197475.04 |
| Authors | Hsueh, F.-C.,Shi, K.,Aihara, H.,Li, F. (deposition date: 2024-01-19, release date: 2024-05-01, Last modification date: 2024-11-13) |
| Primary citation | Hsueh, F.C.,Shi, K.,Mendoza, A.,Bu, F.,Zhang, W.,Aihara, H.,Li, F. Structural basis for raccoon dog receptor recognition by SARS-CoV-2. Plos Pathog., 20:e1012204-e1012204, 2024 Cited by PubMed Abstract: Since the COVID-19 outbreak, raccoon dogs have been suggested as a potential intermediary in transmitting SARS-CoV-2 to humans. To understand their role in the COVID-19 pandemic and the species barrier for SARS-CoV-2 transmission to humans, we analyzed how their ACE2 protein interacts with SARS-CoV-2 spike protein. Biochemical data showed that raccoon dog ACE2 is an effective receptor for SARS-CoV-2 spike protein, though not as effective as human ACE2. Structural comparisons highlighted differences in the virus-binding residues of raccoon dog ACE2 compared to human ACE2 (L24Q, Y34H, E38D, T82M, R353K), explaining their varied effectiveness as receptors for SARS-CoV-2. These variations contribute to the species barrier that exists between raccoon dogs and humans regarding SARS-CoV-2 transmission. Identifying these barriers can help assess the susceptibility of other mammals to SARS-CoV-2. Our research underscores the potential of raccoon dogs as SARS-CoV-2 carriers and identifies molecular barriers that affect the virus's ability to jump between species. PubMed: 38709834DOI: 10.1371/journal.ppat.1012204 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.565 Å) |
Structure validation
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