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.Základní údaje
Originální název
NMR Structure of the N-Terminal Domain of Capsid Protein from the Mason-Pfizer Monkey Virus
Název česky
NMR struktura N-terminální domény kapsidového proteinu Mason-Pfizerova opičího viru
Autoři
MACEK, Pavel (203 Česká republika, domácí), Josef CHMELÍK (203 Česká republika, domácí), Ivana KŘÍŽOVÁ (203 Česká republika), Pavel KADEŘÁVEK (203 Česká republika), Petr PADRTA (203 Česká republika, domácí), Lukáš ŽÍDEK (203 Česká republika, domácí), Marcela WILDOVÁ (203 Česká republika), Romana HADRAVOVÁ (203 Česká republika), Radka CHALOUPKOVÁ (203 Česká republika, domácí), Iva PICHOVÁ (203 Česká republika), Tomáš RUML (203 Česká republika), Michaela RUMLOVÁ (203 Česká republika) a Vladimír SKLENÁŘ (203 Česká republika, garant, domácí)
Vydání
Journal of Molecular Biology, 2009, 0022-2836
Další údaje
Jazyk
angličtina
Typ výsledku
Článek v odborném periodiku
Obor
10600 1.6 Biological sciences
Stát vydavatele
Nizozemské království
Utajení
není předmětem státního či obchodního tajemství
Impakt faktor
Impact factor: 3.871
Kód RIV
RIV/00216224:14310/09:00036514
Organizační jednotka
Přírodovědecká fakulta
UT WoS
000270123600008
Klíčová slova anglicky
M-PMV; betaretroviruses; capsid protein; NMR structure; internal dynamics
Příznaky
Mezinárodní význam, Recenzováno
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.
Česky
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.
Návaznosti
| LC06030, projekt VaV |
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| MSM0021622413, záměr |
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