8PAB
Structures of the ectodomains of Atypical porcine pestivirus solved by long wavelength sulphur SAD
This is a non-PDB format compatible entry.
Summary for 8PAB
| Entry DOI | 10.2210/pdb8pab/pdb |
| Descriptor | Genome polyprotein, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total) |
| Functional Keywords | pestivirus, membrane protein, glycoprotein, viral protein |
| Biological source | Atypical porcine pestivirus |
| Total number of polymer chains | 1 |
| Total formula weight | 29088.26 |
| Authors | |
| Primary citation | Aitkenhead, H.,Riedel, C.,Cowieson, N.,Rumenapf, H.T.,Stuart, D.I.,El Omari, K. Structural comparison of typical and atypical E2 pestivirus glycoproteins. Structure, 32:273-281.e4, 2024 Cited by PubMed Abstract: Pestiviruses, within the family Flaviviridae, are economically important viruses of livestock. In recent years, new pestiviruses have been reported in domestic animals and non-cloven-hoofed animals. Among them, atypical porcine pestivirus (APPV) and Norway rat pestivirus (NRPV) have relatively little sequence conservation in their surface glycoprotein E2. Despite E2 being the main target for neutralizing antibodies and necessary for cell attachment and viral fusion, the mechanism of viral entry remains elusive. To gain further insights into the pestivirus E2 mechanism of action and to assess its diversity within the genus, we report X-ray structures of the pestivirus E2 proteins from APPV and NRPV. Despite the highly divergent structures, both are able to dimerize through their C-terminal domain and contain a solvent-exposed β-hairpin reported to be involved in host receptor binding. Functional analysis of this β-hairpin in the context of BVDV revealed its ability to rescue viral infectivity. PubMed: 38176409DOI: 10.1016/j.str.2023.12.003 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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