2mv4

Solution structure of myristoylated Y28F/Y67F mutant of the Mason-Pfizer monkey virus matrix protein

spinqualitylabelsall models 2mv4 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2mv4 is a 1 chain structure with sequence from Mason-Pfizer monkey virus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: MYR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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