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Zinc-Binding Domain Junín Virus Arenavirus Envelope Glycoprotein

  1. Klára Briknarová

Published Online: 15 JUN 2012

DOI: 10.1002/9781119951438.eibc2056

Encyclopedia of Inorganic and Bioinorganic Chemistry

Encyclopedia of Inorganic and Bioinorganic Chemistry

How to Cite

Briknarová, K. 2012. Zinc-Binding Domain Junín Virus Arenavirus Envelope Glycoprotein. Encyclopedia of Inorganic and Bioinorganic Chemistry. .

Author Information

  1. The University of Montana, Department of Chemistry and Biochemistry and Center for Biomolecular Structure and Dynamics, Missoula, USA

Publication History

  1. Published Online: 15 JUN 2012

Abstract

Arenaviruses are endemic in rodent populations, and several arenavirus species can be transmitted to humans and cause life-threatening hemorrhagic fevers. Entry of arenaviruses into the host cells is mediated by the viral envelope glycoprotein, GPC. Unlike other viral envelope glycoproteins, mature GPC contains a cleaved stable signal peptide (SSP) in addition to the canonical receptor-binding (G1) and transmembrane fusion (G2) subunits. SSP is essential for GPC function and is retained in the complex primarily through interaction with a cytoplasmic zinc-binding domain (ZBD) in G2. The structure of the ZBD from one arenavirus species, Junín, is currently available. The ZBD displays a novel fold and contains two bound zinc ions that are coordinated by four and three residues. The zinc ion that is coordinated by three residues mediates the interaction with the SSP subunit, accepting an invariant cysteine from the cytoplasmic C-terminal tail of SSP as the fourth ligand.

3D Structure

Keywords:

  • zinc-binding domain;
  • Junín virus;
  • arenavirus;
  • envelope glycoprotein