RESEARCH SUPPORT, U.S. GOV'T, P.H.S.
Metal ion chaperone function of the soluble Cu(I) receptor Atx1.
Science 1997 October 32
Reactive and potentially toxic cofactors such as copper ions are imported into eukaryotic cells and incorporated into target proteins by unknown mechanisms. Atx1, a prototypical copper chaperone protein from yeast, has now been shown to act as a soluble cytoplasmic copper(I) receptor that can adopt either a two- or three-coordinate metal center in the active site. Atx1 also associated directly with the Atx1-like cytosolic domains of Ccc2, a vesicular protein defined in genetic studies as a member of the copper-trafficking pathway. The unusual structure and dynamics of Atx1 suggest a copper exchange function for this protein and related domains in the Menkes and Wilson disease proteins.
Full text links
Trending Papers
Oral Anticoagulation in Patients with Chronic Liver Disease.Medicina 2023 Februrary 13
Helicobacter pylori Infection: Current Status and Future Prospects on Diagnostic, Therapeutic and Control Challenges.Antibiotics 2023 January 18
Glucagon-Like Peptide 1 Receptor Agonists Versus Sodium-Glucose Cotransporter 2 Inhibitors for Atherosclerotic Cardiovascular Disease in Patients With Type 2 Diabetes.Cardiology Research 2023 Februrary
Physical interventions to interrupt or reduce the spread of respiratory viruses.Cochrane Database of Systematic Reviews 2023 January 31
Fluid Resuscitation in Patients with Cirrhosis and Sepsis: A Multidisciplinary Perspective.Journal of Hepatology 2023 March 2
Evaluation and Management of Pulmonary Hypertension in Noncardiac Surgery: A Scientific Statement From the American Heart Association.Circulation 2023 March 17
Get seemless 1-tap access through your institution/university
For the best experience, use the Read mobile app
Read by QxMD is copyright © 2021 QxMD Software Inc. All rights reserved. By using this service, you agree to our terms of use and privacy policy.
Get seemless 1-tap access through your institution/university
For the best experience, use the Read mobile app