Commentary abstract
Nature Chemical Biology 4, 148 - 151 (2008)
doi:10.1038/nchembio0308-148
A place for thioether chemistry in cellular copper ion recognition and trafficking
Anna V Davis1 & Thomas V O'Halloran1
- Anna V. Davis is in the Department of Chemistry and Thomas V. O'Halloran is in the Departments of Chemistry and Biochemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston, Illinois 60208, USA. e-mail: t-ohalloran@northwestern.edu
Abstract
Over the last decade, cysteine thiolate ligands have been shown to be critical to the Cu(I) (cuprous) binding chemistry of many cytosolic metallochaperone and metalloregulatory proteins involved in copper physiology. More recently, the thioether group of methionine has begun to emerge as an important Cu(I) ligand for trafficking proteins in more oxidizing cellular environments.
MORE ARTICLES LIKE THIS
These links to content published by NPG are automatically generated.
NEWS AND VIEWS
Copper shares a piece of the πNature Chemical Biology News and Views (01 Feb 2008)
Visualizing tricoordinate copper transferNature Chemical Biology News and Views (01 Jul 2006)
