7C21

Crystal structure of Duvenhage virus phosphoprotein C-terminal domain

7C21 の概要

• エントリーDOI: 10.2210/pdb7c21/pdb
• 分子名称: Phosphoprotein (2 entities in total)
• 機能のキーワード: phosphoprotein, viral protein
• 由来する生物種: Duvenhage virus (DUVV)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12870.82

構造登録者

Sugiyama, A.,Jiang, X.,Maenaka, K.,Yao, M.,Ose, T. (登録日: 2020-05-06, 公開日: 2021-03-17, 最終更新日: 2023-11-29)

主引用文献

Sugiyama, A.,Nomai, T.,Jiang, X.,Minami, M.,Yao, M.,Maenaka, K.,Ito, N.,Gooley, P.R.,Moseley, G.W.,Ose, T.
Structural comparison of the C-terminal domain of functionally divergent lyssavirus P proteins.
Biochem.Biophys.Res.Commun., 529:507-512, 2020

PubMed Abstract: Lyssavirus P protein is a multifunctional protein that interacts with numerous host-cell proteins. The C-terminal domain (CTD) of P is important for inhibition of JAK-STAT signaling enabling the virus to evade host immunity. Several regions on the surface of rabies virus P are reported to interact with host factors. Among them, an extended, discrete hydrophobic patch of P CTD is notable. Although structures of P CTD of two strains of rabies virus, and of mokola virus have been solved, the structure of P CTD for Duvenhage virus, which is functionally divergent from these species for immune evasion function, is not known. Here, we analyze the structures of P CTD of Duvenhage and of a distinct rabies virus strain to gain further insight on the nature and potential function of the hydrophobic surface. Molecular contacts in crystals suggest that the hydrophobic patch is important to intermolecular interactions with other proteins, which differ between the lyssavirus species.

PubMed: 32703459
DOI: 10.1016/j.bbrc.2020.05.195

実験手法

X-RAY DIFFRACTION (1.95 Å)