NMR structure of the mengovirus Leader protein zinc-finger domain

The Leader protein is a defining feature of picornaviruses from the Cardiovirus genus. This protein was recently shown to inhibit cellular nucleocytoplasmic transport through an activity mapped to its zinc-binding region. Here we report the three-dimensional solution structure determined by nuclear...

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Veröffentlicht in:FEBS letters 2008-03, Vol.582 (6), p.896-900
Hauptverfasser: Cornilescu, Claudia C., Porter, Frederick W., Zhao, Kate Qin, Palmenberg, Ann C., Markley, John L.
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Sprache:eng
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Zusammenfassung:The Leader protein is a defining feature of picornaviruses from the Cardiovirus genus. This protein was recently shown to inhibit cellular nucleocytoplasmic transport through an activity mapped to its zinc-binding region. Here we report the three-dimensional solution structure determined by nuclear magnetic resonance (NMR) spectroscopy of this domain (residues 5–28) from mengovirus. The domain forms a CHCC zinc-finger with a fold comprising a β-hairpin followed by a short α-helix that can adopt two different conformations. This structure is divergent from those of other eukaryotic zinc-fingers and instead resembles motifs found in a group of DNA-binding proteins from Archaea.
ISSN:0014-5793
1873-3468
DOI:10.1016/j.febslet.2008.02.023