1H, 13C, and 15N resonance assignment of the N-terminal domain of Mason-Pfizer monkey virus capsid protein, CA 1-140
Jazyk angličtina Země Nizozemsko Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
- MeSH
- izotopy dusíku chemie MeSH
- izotopy uhlíku chemie MeSH
- magnetická rezonanční spektroskopie metody MeSH
- Masonův-Pfizerův opičí virus metabolismus MeSH
- molekulární sekvence - údaje MeSH
- molekulová hmotnost MeSH
- protony MeSH
- sekvence aminokyselin MeSH
- terciární struktura proteinů MeSH
- virové plášťové proteiny chemie MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- izotopy dusíku MeSH
- izotopy uhlíku MeSH
- protony MeSH
- virové plášťové proteiny 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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