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NMR structure of the mengovirus Leader protein zinc‐finger domain
Author(s) -
Cornilescu Claudia C.,
Porter Frederick W.,
Zhao Kate Qin,
Palmenberg Ann C.,
Markley John L.
Publication year - 2008
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2008.02.023
Subject(s) - zinc finger , nuclear magnetic resonance spectroscopy , chemistry , zinc , crystallography , lim domain , biophysics , protein structure , two dimensional nuclear magnetic resonance spectroscopy , biology , biochemistry , nuclear magnetic resonance , stereochemistry , physics , organic chemistry , transcription factor , gene
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.