1H, 13C, and 15N resonance assignment of the N-terminal domain of Mason-Pfizer monkey virus capsid protein, CA 1-140.
Mason-Pfizer monkey virus (M-PMV) belongs to the family of betaretroviruses characterized by the assembly of immature particles within cytoplasm of infected cells in contrast to other retroviruses (e.g. HIV, RSV) that assemble their immature particles at a plasma membrane. Simultaneously with or shortly after budding a virus-encoded protease is activated and the Gag polyprotein is cleaved into three major structural proteins: matrix (MA), capsid (CA), and nucleocapsid (NC) protein. Mature retroviral CA proteins consist of two independently folded structural domains: N-terminal domain (NTD) and C-terminal dimerization domain (CTD), separated by a flexible linker. As a first step toward the solution structure elucidation, we present nearly complete backbone and side-chain 1H, 13C and 15N resonance assignment of the M-PMV NTD CA.
Macek
Pavel
P
Faculty of Science, National Centre for Biomolecular Research, Masaryk University, Kotlárská 2, 61137 Brno, Czech Republic.
Zídek
Lukás
L
Rumlová
Michaela
M
Pichová
Iva
I
Sklenár
Vladimír
V
D000595:Amino Acid Sequence; D036022:Capsid Proteins / Q000737:chemistry*; D002247:Carbon Isotopes / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D016093:Mason-Pfizer monkey virus / Q000378:metabolism*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009587:Nitrogen Isotopes / Q000737:chemistry; D017434:Protein Structure, Tertiary; D011522:Protons
D036022:Capsid Proteins; D002247:Carbon Isotopes; D009587:Nitrogen Isotopes; D011522:Protons