Journal
CURRENT OPINION IN CHEMICAL BIOLOGY
Volume 4, Issue 2, Pages 140-147Publisher
ELSEVIER SCI LTD
DOI: 10.1016/S1367-5931(99)00066-6
Keywords
-
Categories
Funding
- NIGMS NIH HHS [R01 GM054111] Funding Source: Medline
Ask authors/readers for more resources
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available