Počet záznamů: 1

NMR structure of the N-terminal domain of capsid protein from the Mason-Pfizer monkey virus

  1. 1.
    0334395 - UOCHB-X 2010 RIV GB eng J - Článek v odborném periodiku
    Macek, Pavel - Chmelík, Josef - Křížová, Ivana - Kadeřávek, P. - Padrta, P. - Žídek, L. - Wildová, Marcela - Hadravová, Romana - Chaloupková, R. - Pichová, Iva - Ruml, T. - Rumlová, Michaela - Sklenář, V.
    NMR structure of the N-terminal domain of capsid protein from the Mason-Pfizer monkey virus.
    Journal of Molecular Biology. Roč. 392, č. 1 (2009), s. 100-114 ISSN 0022-2836
    Grant CEP: GA MŠk LC545; GA MŠk 1M0508; GA ČR GA204/09/1388; GA ČR GESCO/06/E001
    Grant ostatní: GA MŠk(CZ) 1M0520; MŠk(CZ) LC06030
    Výzkumný záměr: CEZ:AV0Z40550506; CEZ:AV0Z50200510
    Klíčová slova: M-PMV * betaretroviruses * capsid protein * NMR structure * internal dynamics
    Kód oboru RIV: CE - Biochemie
    Impakt faktor: 3.871, rok: 2009

    The high-resolution structure of the N-terminal domain of the retroviral capsid protein of Mason-Pfizer monkey virus has been determined by NMR. The structure is characterized by a six alpha-helices and an N-terminal beta-hairpin, stabilized by an interaction of Pro1 and Asp57. NMR data obtained for two mutants where beta-hairpin stabilization was disrupted (P1NTDCA and D57ANTDCA) were compared with those for the wild-type. Observed structural changes were supported by biochemical studies.
    Trvalý link: http://hdl.handle.net/11104/0179142