Superoxide dismutase catalyzes the disproportionation of superoxide to hydrogen peroxide and dioxygen. For activity, this exzyme requires one dimetallic Cu,Zn center per subunit. In yeast, the insertion of the copper into superoxide dismutase (Sod1) only occurs in the presence of the copper chaperone protein Lys7. The objective of this proposal is to solve the three dimensional structures of Lys7, with and without the metal ions, and Lys7 complexed with Sod1. In humans, Sod1 has been linked to familial amyotrophic lateral sclerosis (Lou Gehrig's Disease), and a detailed understanding of the mechanism of copper insertion should lead to the development of new therapies for this disease.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Postdoctoral Individual National Research Service Award (F32)
Project #
1F32GM019973-01
Application #
2861475
Study Section
Biophysical Chemistry Study Section (BBCB)
Project Start
1999-06-01
Project End
Budget Start
1999-06-01
Budget End
2000-05-31
Support Year
1
Fiscal Year
1999
Total Cost
Indirect Cost
Name
Northwestern University at Chicago
Department
Biochemistry
Type
Schools of Arts and Sciences
DUNS #
City
Evanston
State
IL
Country
United States
Zip Code
60201