Structural highlights
Function
[GAG_MPMV] p10 is the matrix protein. P14 is the nucleocapsid protein. p27 is the capsid protein.
Publication Abstract from PubMed
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.
Resonance assignments of the myristoylated Y28F/Y67F mutant of the Mason-Pfizer monkey virus matrix protein.,Dolezal M, Hrabal R, Ruml T, Rumlova M Biomol NMR Assign. 2015 Mar 15. PMID:25773138[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ 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. 2015 Mar 15. PMID:25773138 doi:http://dx.doi.org/10.1007/s12104-014-9580-0
