Journal
BIOMOLECULAR NMR ASSIGNMENTS
Volume 2, Issue 1, Pages 43-45Publisher
SPRINGER
DOI: 10.1007/s12104-008-9080-1
Keywords
NMR; assignment; capsid protein; Mason-Pfizer monkey virus
Categories
Funding
- Ministry of Education, Youth and Sports of the Czech Republic [MSM0021622413, LC06030, LC545, M6138896301, Z 4055905]
Ask authors/readers for more resources
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 H-1, N-15 and C-13 resonance assignment of the M-PMV NTD CA.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available