2K36

Structure ensemble Backbone and side-chain 1H, 13C, and 15N Chemical Shift Assignments, 1H-15N RDCs and 1H-1H nOe restraints for protein K7 from the Vaccinia virus

2K36 の概要

• エントリーDOI: 10.2210/pdb2k36/pdb
• NMR情報: BMRB: 15740
• 分子名称: Protein K7 (1 entity in total)
• 機能のキーワード: protein, viral protein
• 由来する生物種: Vaccinia virus (VACV)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17488.90

構造登録者

Kalverda, A.P.,Thompson, G.S.,Vogel, A.,Schr der, M.,Bowie, A.G.,Khan, A.R.,Homans, S.W. (登録日: 2008-04-22, 公開日: 2008-10-28, 最終更新日: 2024-05-01)

主引用文献

Kalverda, A.P.,Thompson, G.S.,Vogel, A.,Schroder, M.,Bowie, A.G.,Khan, A.R.,Homans, S.W.
Poxvirus K7 protein adopts a Bcl-2 fold: biochemical mapping of its interactions with human DEAD box RNA helicase DDX3.
J.Mol.Biol., 385:843-853, 2009

PubMed Abstract: Poxviruses have evolved numerous strategies to evade host innate immunity. Vaccinia virus K7 is a 149-residue protein with previously unknown structure that is highly conserved in the orthopoxvirus family. K7 bears sequence and functional similarities to A52, which interacts with interleukin receptor-associated kinase 2 and tumor necrosis factor receptor-associated factor 6 to suppress nuclear factor kappaB activation and to stimulate the secretion of the anti-inflammatory cytokine interleukin-10. In contrast to A52, K7 forms a complex with DEAD box RNA helicase DDX3, thereby suppressing DDX3-mediated ifnb promoter induction. We determined the NMR solution structure of K7 to provide insight into the structural basis for poxvirus antagonism of innate immune signaling. The structure reveals an alpha-helical fold belonging to the Bcl-2 family despite an unrelated primary sequence. NMR chemical-shift mapping studies have localized the binding surface for DDX3 on a negatively charged face of K7. Furthermore, thermodynamic studies have mapped the K7-binding region to a 30-residue N-terminal fragment of DDX3, ahead of the core RNA helicase domains.

PubMed: 18845156
DOI: 10.1016/j.jmb.2008.09.048

実験手法

SOLUTION NMR