Structure and chemistry of the copper chaperone proteins

Amy C. Rosenzweig*, Thomas V. O'Halloran

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

156 Scopus citations


Major advances have been made in the past year towards an understanding of the structure and chemistry of copper chaperone proteins. Three-dimensional structures of Atx1, CopZ, yCCS, and hCCSdll were determined, and reveal a remarkable structural similarity between chaperones and target proteins. In addition, biochemical studies of CCS suggested that chaperones are required in vivo because intracellular copper concentrations are extremely low and also indicated that copper transfer occurs via a direct protein-protein interaction.

Original languageEnglish (US)
Pages (from-to)140-147
Number of pages8
JournalCurrent Opinion in Chemical Biology
Issue number2
StatePublished - Apr 1 2000

ASJC Scopus subject areas

  • Analytical Chemistry
  • Biochemistry

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