Mutation detail:
| Mutation site | G11A |
| Virus | SARS-CoV |
Mutation level  |
Amino acid level |
| Gene/protein/region type | S Protein |
| Gene ID | 1489668 |
| Country | - |
| Mutation type |
nonsynonymous mutation |
| Genotype/subtype/clade | - |
| Sample |
cell line |
| Variants | - |
| Viral reference sequence | AY291315.1 |
| Drug/antibody/vaccine | - |
| Transmissibility |
- |
| Transmission mechanism | - |
| Pathogenicity |
decrease |
| Pathogenicity mechanism | In this study, we showed that mutation of the dimer-interface residue Gly-11 to alanine entirely abolished the activity of SARS-CoV 3CLpro. Subsequently, we determined the crystal structure of this mutant and discovered a complete crystallographic dimer d |
| Immune escape mutation | - |
| Immune escape mechanism | - |
| RT-PCR primers probes | - |
Protein detail:
| Protein name | spike glycoprotein |
| Uniprot protein ID | P59594 |
| Protein length | 1255 amino acids |
| Protein description | The spike protein of SARS coronaviruses is a protein composed of three polypeptide chains and it contains two domains, S1 and S2. The S1 domain binds the host cell receptors, while the S2 domain is responsible for the fusion of the virus with the host cell membrane. Between S1 and S2, there is a hinge region which is targeted by the host cell proteases. |
Literature information:
| Pubmed ID | 17977841 |
| Clinical information | No |
| Disease | - |
| Published year | 2008 |
| Journal | JOURNAL OF BIOLOGICAL CHEMISTRY |
| Title | Mutation of Gly-11 on the dimer interface results in the complete crystallographic dimer dissociation of severe acute respiratory syndrome coronavirus 3C-like protease: crystal structure with molecular dynamics simulations |
| Author | Shuai Chen, Tiancen Hu, Jian Zhang, Jing Chen, Kaixian Chen |
| Evidence | In this study, we showed that mutation of the dimer-interface residue Gly-11 to alanine entirely abolished the activity of SARS-CoV 3CLpro. |