NMR structure of the mengovirus Leader protein zinc-finger domain |
| |
Authors: | Cornilescu Claudia C Porter Frederick W Zhao Kate Qin Palmenberg Ann C Markley John L |
| |
Affiliation: | a Department of Biochemistry, University of Wisconsin-Madison, Madison, WI 53706-1544, United States b Center for Eukaryotic Structural Genomics, University of Wisconsin-Madison, Madison, WI 53706-1544, United States c Institute for Molecular Virology, University of Wisconsin-Madison, Madison, WI 53706, United States |
| |
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 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. |
| |
Keywords: | EMCV, encephalomyocarditis virus GDP, guanosine diphosphate GST, glutathione S-transferase GTP, guanosine triphosphate L, Leader protein LM, Leader protein from Mengovirus MALDI-MS, matrix assisted laser desorption ionization- mass spectrometry NLS, nuclear localization signal NMR, nuclear magnetic resonance rmsd, root mean square deviation SDS-PAGE, sodium dodecyl sulfate-polyacrylamide gel electrophoresis TMEV, Theiler&rsquo s murine encephalomyocarditis virus |
本文献已被 ScienceDirect PubMed 等数据库收录! |
|