Mutation detail:
| Mutation site | C1199W |
| Virus | Human rhinovirus |
Mutation level  |
Amino acid level |
| Gene/protein/region type | VP1 |
| Gene ID | 1461213 |
| Country | - |
| Mutation type |
nonsynonymous mutation |
| Genotype/subtype/clade | B |
| Sample |
cell line |
| Variants | - |
| Viral reference sequence | NC_001490.1 |
| Drug/antibody/vaccine | - |
| Transmissibility |
- |
| Transmission mechanism | - |
| Pathogenicity |
- |
| Pathogenicity mechanism | - |
| Immune escape mutation | - |
| Immune escape mechanism | - |
| RT-PCR primers probes | - |
Protein detail:
| Protein name | Capsid Protein VP1 |
| Uniprot protein ID | P03303 |
| Protein length | 289 amino acids |
| Protein description | VP1 forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome. Capsid protein VP1 mainly forms the vertices of the capsid. Capsid protein VP1 interacts with host ICAM1 to provide virion attachment to target host cells. |
Literature information:
| Pubmed ID | 14517058 |
| Clinical information | No |
| Disease | - |
| Published year | 2003 |
| Journal | Virology |
| Title | Human rhinovirus capsid dynamics is controlled by canyon flexibility |
| Author | Nichole Reisdorph,John J Thomas,Umesh Katpally,Elaine Chase,Ken Harris |
| Evidence | The bottom panel is a stereo diagram of the WIN 52084/HRV14 complex with the V1188M and C1200W mutations modeled to show how they fill the drug binding cavity and sterically block WIN binding |