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FEBS Lett. 2008 Mar 19;582(6):896-900. doi: 10.1016/j.febslet.2008.02.023. Epub 2008 Feb 20.

NMR structure of the mengovirus Leader protein zinc-finger domain.

Author information

1
Department of Biochemistry, University of Wisconsin-Madison, Madison, WI 53706-1544, USA. cclaudia@nmrfam.wisc.edu <cclaudia@nmrfam.wisc.edu>

Abstract

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 beta-hairpin followed by a short alpha-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.

PMID:
18291103
DOI:
10.1016/j.febslet.2008.02.023
[Indexed for MEDLINE]
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