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Preliminary crystallographic characterization of an RNA helicase from Kunjin virus (Articolo in rivista)

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Preliminary crystallographic characterization of an RNA helicase from Kunjin virus (Articolo in rivista) (literal)

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Mastrangelo, E; Bollati, M; Milani, M; Brisbarre, N; de Lamballerie, X; Coutard, B; Canard, B; Khromykh, A; Bolognesi, M (2006)
Preliminary crystallographic characterization of an RNA helicase from Kunjin virus
in Acta crystallographica. Section F
(literal)

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Mastrangelo, E; Bollati, M; Milani, M; Brisbarre, N; de Lamballerie, X; Coutard, B; Canard, B; Khromykh, A; Bolognesi, M (literal)

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Univ Milan, CNR INFM, Dept Biomol Sci & Biotechnol, I-20133 Milan, Italy; Fac Med Marseille, Unite Virus Emergents, F-13005 Marseille, France; ESIL, CNRS, UMR 6098, Lab Architecture & Fonct Macromol Biol, F-13288 Marseille, France; Univ Queensland, Sch Mol & Microbiol Sci, RNA Virol Lab, Brisbane, Qld 4072, Australia (literal)

Titolo

Preliminary crystallographic characterization of an RNA helicase from Kunjin virus (literal)

Abstract

Kunjin virus is a member of the Flavivirus genus and is an Australian variant of West Nile virus. The C-terminal domain of the Kunjin virus NS3 protein displays helicase activity. The protein is thought to separate daughter and template RNA strands, assisting the initiation of replication by unwinding RNA secondary structure in the 3' nontranslated region. Expression, purification and preliminary crystallographic characterization of the NS3 helicase domain are reported. It is shown that Kunjin virus helicase may adopt a dimeric assembly in absence of nucleic acids, oligomerization being a means to provide the helicases with multiple nucleic acid-binding capability, facilitating translocation along the RNA strands. Kunjin virus NS3 helicase domain is an attractive model for studying the molecular mechanisms of flavivirus replication, while simultaneously providing a new basis for the rational development of anti-flaviviral compounds. (literal)

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