NMR structure of the N-terminal domain of capsid protein from the mason-pfizer monkey virus
Language English Country Netherlands Media print-electronic
Document type Comparative Study, Journal Article, Research Support, N.I.H., Extramural, Research Support, Non-U.S. Gov't
Grant support
5CA 27834
NCI NIH HHS - United States
PubMed
19527730
DOI
10.1016/j.jmb.2009.06.029
PII: S0022-2836(09)00736-0
Knihovny.cz E-resources
- MeSH
- Mason-Pfizer monkey virus chemistry MeSH
- Models, Molecular MeSH
- Mutant Proteins chemistry MeSH
- Nuclear Magnetic Resonance, Biomolecular methods MeSH
- Sequence Deletion MeSH
- Amino Acid Substitution MeSH
- Protein Structure, Tertiary MeSH
- Capsid Proteins chemistry MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Research Support, N.I.H., Extramural MeSH
- Comparative Study MeSH
- Names of Substances
- Mutant Proteins MeSH
- Capsid Proteins MeSH
The high-resolution structure of the N-terminal domain (NTD) of the retroviral capsid protein (CA) of Mason-Pfizer monkey virus (M-PMV), a member of the betaretrovirus family, has been determined by NMR. The M-PMV NTD CA structure is similar to the other retroviral capsid structures and is characterized by a six alpha-helix bundle and an N-terminal beta-hairpin, stabilized by an interaction of highly conserved residues, Pro1 and Asp57. Since the role of the beta-hairpin has been shown to be critical for formation of infectious viral core, we also investigated the functional role of M-PMV beta-hairpin in two mutants (i.e., DeltaP1NTDCA and D57ANTDCA) where the salt bridge stabilizing the wild-type structure was disrupted. NMR data obtained for these mutants were compared with those obtained for the wild type. The main structural changes were observed within the beta-hairpin structure; within helices 2, 3, and 5; and in the loop connecting helices 2 and 3. This observation is supported by biochemical data showing different cleavage patterns of the wild-type and the mutated capsid-nucleocapsid fusion protein (CANC) by M-PMV protease. Despite these structural changes, the mutants with disrupted salt bridge are still able to assemble into immature, spherical particles. This confirms that the mutual interaction and topology within the beta-hairpin and helix 3 might correlate with the changes in interaction between immature and mature lattices.
References provided by Crossref.org
Structure of the immature HIV-1 capsid in intact virus particles at 8.8 Å resolution
Role of Mason-Pfizer monkey virus CA-NC spacer peptide-like domain in assembly of immature particles
In vitro assembly of virus-like particles of a gammaretrovirus, the murine leukemia virus XMRV
PDB
2KGF
