4.0 Article

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

Journal

BIOMOLECULAR NMR ASSIGNMENTS
Volume 9, Issue 2, Pages 229-233

Publisher

SPRINGER
DOI: 10.1007/s12104-014-9580-0

Keywords

Isotopic labeling; Matrix protein; M-PMV; Myristoylation; Resonance assignment; Reverse labeling

Funding

  1. Czech Science Foundation [P302/12/1895]

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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.

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