2MV4
Solution structure of myristoylated Y28F/Y67F mutant of the Mason-Pfizer monkey virus matrix protein
Summary for 2MV4
| Entry DOI | 10.2210/pdb2mv4/pdb |
| NMR Information | BMRB: 25087 |
| Descriptor | Matrix protein p10 (1 entity in total) |
| Functional Keywords | gag, matrix protein, m-pmv, myristoyl switch, myristoylation, retrovirus, viral protein |
| Biological source | Mason-Pfizer monkey virus (MPMV) |
| Cellular location | Matrix protein p10: Virion . Capsid protein p27: Virion . Nucleocapsid protein p14: Virion : P07567 |
| Total number of polymer chains | 1 |
| Total formula weight | 14891.99 |
| Authors | Dolezal, M.,Hrabal, R. (deposition date: 2014-09-23, release date: 2015-04-01, Last modification date: 2022-12-21) |
| Primary citation | 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 Cited by 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: 25773138DOI: 10.1007/s12104-014-9580-0 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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