Mutation detail:
| Mutation site | R426A |
| 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 | AY274119.3 |
| Drug/antibody/vaccine | - |
| Transmissibility |
hinder |
| Transmission mechanism | In the structure of the S RBD-ACE2 complex two of the mutants with very significantly reduced binding to ACE2, R426A and N473A, make contacts with ACE2 residues and are completely exposed (Table1). |
| Pathogenicity |
- |
| Pathogenicity mechanism | - |
| 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 | 16122388 |
| Clinical information | No |
| Disease | - |
| Published year | 2005 |
| Journal | VIROLOGY JOURNAL |
| Title | The SARS coronavirus S glycoprotein receptor binding domain: fine mapping and functional characterization |
| Author | Samitabh Chakraborti, Ponraj Prabakaran, Xiaodong Xiao, Dimiter S Dimitrov |
| Evidence | In the structure of the S RBD-ACE2 complex two of the mutants with very significantly reduced binding to ACE2, R426A and N473A, make contacts with ACE2 residues and are completely exposed (Table1). |