Detailed Information on Publication Record
2009
NMR Structure of the N-Terminal Domain of Capsid Protein from the Mason-Pfizer Monkey Virus
MACEK, Pavel, Josef CHMELÍK, Ivana KŘÍŽOVÁ, Pavel KADEŘÁVEK, Petr PADRTA et. al.Basic information
Original name
NMR Structure of the N-Terminal Domain of Capsid Protein from the Mason-Pfizer Monkey Virus
Name in Czech
NMR struktura N-terminální domény kapsidového proteinu Mason-Pfizerova opičího viru
Authors
MACEK, Pavel (203 Czech Republic, belonging to the institution), Josef CHMELÍK (203 Czech Republic, belonging to the institution), Ivana KŘÍŽOVÁ (203 Czech Republic), Pavel KADEŘÁVEK (203 Czech Republic), Petr PADRTA (203 Czech Republic, belonging to the institution), Lukáš ŽÍDEK (203 Czech Republic, belonging to the institution), Marcela WILDOVÁ (203 Czech Republic), Romana HADRAVOVÁ (203 Czech Republic), Radka CHALOUPKOVÁ (203 Czech Republic, belonging to the institution), Iva PICHOVÁ (203 Czech Republic), Tomáš RUML (203 Czech Republic), Michaela RUMLOVÁ (203 Czech Republic) and Vladimír SKLENÁŘ (203 Czech Republic, guarantor, belonging to the institution)
Edition
Journal of Molecular Biology, 2009, 0022-2836
Other information
Language
English
Type of outcome
Článek v odborném periodiku
Field of Study
10600 1.6 Biological sciences
Country of publisher
Netherlands
Confidentiality degree
není předmětem státního či obchodního tajemství
Impact factor
Impact factor: 3.871
RIV identification code
RIV/00216224:14310/09:00036514
Organization unit
Faculty of Science
UT WoS
000270123600008
Keywords in English
M-PMV; betaretroviruses; capsid protein; NMR structure; internal dynamics
Tags
International impact, Reviewed
Změněno: 10/3/2011 13:05, prof. RNDr. Vladimír Sklenář, DrSc.
V originále
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.
In Czech
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.
Links
| LC06030, research and development project |
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| MSM0021622413, plan (intention) |
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