Resonance assignments of the myristoylated Y28F/Y67F mutant of the Mason-Pfizer monkey virus matrix protein

0449387 - ÚOCHB 2016 RIV DE eng J - Článek v odborném periodiku
Doležal, Michal - Hrabal, R. - Ruml, T. - Rumlová, Michaela
Resonance assignments of the myristoylated Y28F/Y67F mutant of the Mason-Pfizer monkey virus matrix protein.
Biomolecular NMR Assignments. Roč. 9, č. 2 (2015), s. 229-233. ISSN 1874-2718. E-ISSN 1874-270X
Institucionální podpora: RVO:61388963
Klíčová slova: isotopic labeling * matrix protein * M-PMV * myristoylation * resonance assignment * reverse labeling
Kód oboru RIV: CE - Biochemie
Impakt faktor: 0.687, rok: 2015

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.
Trvalý link: http://hdl.handle.net/11104/0251099