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.

Department of Biochemistry and Microbiology University of Chemistry and Technology Prague Technická 5 16628 Prague Czech Republic

Department of Biotechnology University of Chemistry and Technology Prague Technická 5 16628 Prague Czech Republic

Institute of Organic Chemistry and Biochemistry v v i IOCB and Gilead Research Center Academy of Sciences of the Czech Republic Flemingovo nám 2 166 10 Prague Czech Republic

Laboratory of NMR Spectroscopy University of Chemistry and Technology Prague Technická 5 16628 Prague Czech Republic

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