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NMR structure of the N-terminal domain of capsid protein from the Mason-Pfizer monkey virus
- 1.0334395 - ÚOCHB 2010 RIV GB eng J - Journal Article
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. E-ISSN 1089-8638
R&D Projects: GA MŠMT LC545; GA MŠMT 1M0508; GA ČR GA204/09/1388; GA ČR GESCO/06/E001
Grant - others:GA MŠk(CZ) 1M0520; MŠk(CZ) LC06030
Program: 1M; LC
Institutional research plan: CEZ:AV0Z40550506; CEZ:AV0Z50200510
Keywords : M-PMV * betaretroviruses * capsid protein * NMR structure * internal dynamics
Subject RIV: CE - Biochemistry
Impact factor: 3.871, year: 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.
Permanent Link: http://hdl.handle.net/11104/0179142
Number of the records: 1