2MV4

Solution structure of myristoylated Y28F/Y67F mutant of the Mason-Pfizer monkey virus matrix protein

2MV4 の概要

• エントリーDOI: 10.2210/pdb2mv4/pdb
• NMR情報: BMRB: 25087
• 分子名称: Matrix protein p10 (1 entity in total)
• 機能のキーワード: gag, matrix protein, m-pmv, myristoyl switch, myristoylation, retrovirus, viral protein
• 由来する生物種: Mason-Pfizer monkey virus (MPMV)
• 細胞内の位置: Matrix protein p10: Virion . Capsid protein p27: Virion . Nucleocapsid protein p14: Virion : P07567
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14891.99

構造登録者

Dolezal, M.,Hrabal, R. (登録日: 2014-09-23, 公開日: 2015-04-01, 最終更新日: 2022-12-21)

主引用文献

Dolezal, M.,Hrabal, R.,Ruml, T.,Rumlova, M.
Resonance assignments of the myristoylated Y28F/Y67F mutant of the Mason-Pfizer monkey virus matrix protein.
Biomol.Nmr Assign., 9:229-233, 2015

PubMed Abstract: The matrix protein (MA) of the Mason-Pfizer monkey virus (M-PMV) plays a key role in the transport and budding of immature retroviral particles from the host cell. Natural N-terminal myristoylation of MA is essential for the targeting of the particles to the plasma membrane and participates in the interaction of MA with membranes phospholipids. The mutation Y28F/Y67F in MA reduces budding and thus causes the accumulation of viral particles under the cytoplasmic membrane. To investigate the impact of Y28F/Y67F mutation on the structure of MA, we prepared this protein in amount and quality suitable for NMR spectroscopy. We report backbone, side-chain and myristoyl residue assignments of the Y28F/Y67F mutant of the M-PMV matrix protein, which will be used to study the interaction with membrane phospholipids and to determine the structure of the mutant matrix protein.

PubMed: 25773138
DOI: 10.1007/s12104-014-9580-0

実験手法

SOLUTION NMR