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Mechanisms of Copper Chaperone Proteins

  • Robert A. Pufahl
  • Thomas V. O’Halloran

Abstract

Little is known about the chemistry and biology involved in getting a metal such as copper (Cu) to the right place in a cell. Recently, several members of an emerging class of proteins have been proposed to play a role in guiding and protecting metal ions inside cells, and ultimately delivering these cofactors to specific targets. The copper escort function for one of the yeast proteins, Atxl, has been established (Pufahl et al., 1997). A similar function has been proposed for another yeast protein, Lys7, which shares some sequence similarity to Atxl, but is thought to deliver copper to another target within the cell (Culotta et al., 1997). This review summarizes recent insights into the biological chemistry of these two prototypical metal ion chaperone proteins.

Keywords

Chaperone Protein Copper Binding Menkes Disease Copper Chaperone LYS7 Gene 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1999

Authors and Affiliations

  • Robert A. Pufahl
    • 1
  • Thomas V. O’Halloran
    • 2
  1. 1.Department of ChemistryEvanstonUSA
  2. 2.Department of Biochemistry, Molecular, Biology and Cell BiologyNorthwestern UniversityEvanstonUSA

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