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NMR structure of the mengovirus Leader protein zinc-finger domain

Claudia C Cornilescu1, Frederick W Porter, Kate Qin Zhao

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

FEBS Letters
|February 23, 2008
PubMed

Insights

The Leader protein

Area of Science:

  • Virology
  • Structural Biology
  • Molecular Biology

Background:

  • Picornaviruses, particularly the Cardiovirus genus, possess a unique Leader protein.
  • This protein is known to disrupt nucleocytoplasmic transport via its zinc-binding region.

Purpose of the Study:

  • To determine the 3D solution structure of the mengovirus Leader protein's zinc-binding domain.
  • To understand the structural basis for its inhibition of nucleocytoplasmic transport.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) spectroscopy was used to determine the structure.
  • The study focused on residues 5-28 of the mengovirus Leader protein.

Main Results:

  • The domain adopts a CHCC zinc-finger fold.
  • It features a beta-hairpin followed by an alpha-helix, capable of two conformations.
  • This fold is distinct from eukaryotic zinc-fingers and resembles archaeal DNA-binding motifs.

Conclusions:

  • The unique structure of the Cardiovirus Leader protein's zinc-finger domain provides insights into its function.
  • Its structural divergence suggests a potentially novel mechanism for inhibiting nucleocytoplasmic transport.
  • The resemblance to archaeal motifs may indicate evolutionary connections or functional analogies.

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