Copper delivery by metallochaperone proteins

Amy C Rosenzweig*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

230 Scopus citations

Abstract

Copper is an essential element in all living organisms, serving as a cofactor for many important proteins and enzymes. Metallochaperone proteins deliver copper ions to specific physiological partners by direct protein - protein interactions. The Atxl-like chaperones transfer copper to intracellular copper transporters, and the CCS chaperones shuttle copper to copper,zinc superoxide dismutase. Crystallographic studies of these two copper chaperone families have provided insights into metal binding and target recognition by metallochaperones and have led to detailed molecular models for the copper transfer mechanism.

Original languageEnglish (US)
Pages (from-to)119-128
Number of pages10
JournalAccounts of Chemical Research
Volume34
Issue number2
DOIs
StatePublished - Mar 3 2001

ASJC Scopus subject areas

  • Chemistry(all)

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