9HC5
Structure of Tulane virus
Summary for 9HC5
| Entry DOI | 10.2210/pdb9hc5/pdb |
| EMDB information | 52037 |
| Descriptor | Capsid protein (1 entity in total) |
| Functional Keywords | capsid, tulane virus, calicivirus, virus |
| Biological source | Tulane virus |
| Total number of polymer chains | 3 |
| Total formula weight | 173670.17 |
| Authors | Bhella, D.,Conley, M.J. (deposition date: 2024-11-08, release date: 2024-12-04, Last modification date: 2025-01-22) |
| Primary citation | Lewis, C.B.,Sherry, L.,Conley, M.J.,Nakashima, M.,Akbar, S.,Govindan, N.,Hosie, M.J.,Bhella, D. Conformational Flexibility in Capsids Encoded by the Caliciviridae . Viruses, 16:-, 2024 Cited by PubMed Abstract: Caliciviruses are a diverse group of non-enveloped, positive-sense RNA viruses with a wide range of hosts and transmission routes. Norovirus is the most well-known member of the ; the acute gastroenteritis caused by human norovirus (HuNoV), for example, frequently results in closures of hospital wards and schools during the winter months. One area of calicivirus biology that has gained increasing attention over the past decade is the conformational flexibility exhibited by the protruding (P) domains of the major capsid protein VP1. This was observed in structure analyses of capsids encoded by many species and is often a consequence of environmental cues such as metal ions, changes to pH, or receptor/co-factor engagement. This review summarises the current understanding of P-domain flexibility, discussing the role this region plays in caliciviral infection and immune evasion, and highlighting potential avenues for further investigation. PubMed: 39772145DOI: 10.3390/v16121835 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.6 Å) |
Structure validation
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