Resonance assignments of the myristoylated Y28F/Y67F mutant of the Mason-Pfizer monkey virus matrix protein
Language English Country Netherlands Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
25773138
DOI
10.1007/s12104-014-9580-0
PII: 10.1007/s12104-014-9580-0
Knihovny.cz E-resources
- Keywords
- Isotopic labeling, M-PMV, Matrix protein, Myristoylation, Resonance assignment, Reverse labeling,
- MeSH
- Myristic Acid metabolism MeSH
- Mason-Pfizer monkey virus metabolism MeSH
- Mutant Proteins chemistry MeSH
- Nuclear Magnetic Resonance, Biomolecular * MeSH
- Viral Matrix Proteins chemistry MeSH
- Proton Magnetic Resonance Spectroscopy MeSH
- Protein Structure, Secondary MeSH
- Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Myristic Acid MeSH
- Mutant Proteins MeSH
- Viral Matrix Proteins MeSH
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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