8PAB

Structures of the ectodomains of Atypical porcine pestivirus solved by long wavelength sulphur SAD

これはPDB形式変換不可エントリーです。

8PAB の概要

• エントリーDOI: 10.2210/pdb8pab/pdb
• 分子名称: Genome polyprotein, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• 機能のキーワード: pestivirus, membrane protein, glycoprotein, viral protein
• 由来する生物種: Atypical porcine pestivirus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 29088.26

構造登録者

Aitkenhead, H.,Stuart, D.I.,El Omari, K. (登録日: 2023-06-07, 公開日: 2024-03-27, 最終更新日: 2024-11-20)

主引用文献

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

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: 38176409
DOI: 10.1016/j.str.2023.12.003

実験手法

X-RAY DIFFRACTION (1.8 Å)