1H, 13C, and 15N resonance assignment of the N-terminal domain of Mason-Pfizer monkey virus capsid protein, CA 1-140
Language English Country Netherlands Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
- MeSH
- Nitrogen Isotopes chemistry MeSH
- Carbon Isotopes chemistry MeSH
- Magnetic Resonance Spectroscopy methods MeSH
- Mason-Pfizer monkey virus metabolism MeSH
- Molecular Sequence Data MeSH
- Molecular Weight MeSH
- Protons MeSH
- Amino Acid Sequence MeSH
- Protein Structure, Tertiary MeSH
- Capsid Proteins chemistry MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Nitrogen Isotopes MeSH
- Carbon Isotopes MeSH
- Protons MeSH
- Capsid Proteins MeSH
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.
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