Journal
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
Volume 1764, Issue 1, Pages 5-12Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbapap.2005.11.003
Keywords
synuclein; Parkinson's disease; copper binding; protein aggregation
Categories
Funding
- NATIONAL INSTITUTE ON AGING [R37AG019391, R01AG025440, R01AG019391] Funding Source: NIH RePORTER
- NIA NIH HHS [R01 AG025440, R37 AG019391, R01 AG019391-06, R01 AG025440-01A1, AG019391, R01 AG019391] Funding Source: Medline
Ask authors/readers for more resources
Copper binding to the Parkinson disease-linked protein alpha-synuclein (aS) has been shown to accelerate its oligomerization in vitro and may therefore play a role in aS-mediated pathology in vivo. We use NMR spectroscopy to identify a number of independent copper binding sites in both the lipid-binding N-terminal domain and the highly acidic C-terminal domain of aS. Most of the sites appear to involve negatively charged amino acid side chains, but binding is also observed to the sole histidine residue located at position 50 and to the N-terminal amino group. Both the N-terminal and the histidine sites, as well as the sites in the C-terminal tail, can also bind copper in the more highly structured conformation adopted by aS upon binding to detergent micelles or lipid vesicles. There is no evidence for the formation of any sites requiring long-range order in the protein. (c) 2005 Elsevier B.V. All rights reserved.
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