Citation
Barnham, Kevin J., et al. "Structure of the Alzheimer's Disease Amyloid Precursor Protein Copper Binding Domain. a Regulator of Neuronal Copper Homeostasis." The Journal of Biological Chemistry, vol. 278, no. 19, 2003, pp. 17401-7.
Barnham KJ, McKinstry WJ, Multhaup G, et al. Structure of the Alzheimer's disease amyloid precursor protein copper binding domain. A regulator of neuronal copper homeostasis. J Biol Chem. 2003;278(19):17401-7.
Barnham, K. J., McKinstry, W. J., Multhaup, G., Galatis, D., Morton, C. J., Curtain, C. C., Williamson, N. A., White, A. R., Hinds, M. G., Norton, R. S., Beyreuther, K., Masters, C. L., Parker, M. W., & Cappai, R. (2003). Structure of the Alzheimer's disease amyloid precursor protein copper binding domain. A regulator of neuronal copper homeostasis. The Journal of Biological Chemistry, 278(19), 17401-7.
Barnham KJ, et al. Structure of the Alzheimer's Disease Amyloid Precursor Protein Copper Binding Domain. a Regulator of Neuronal Copper Homeostasis. J Biol Chem. 2003 May 9;278(19):17401-7. PubMed PMID: 12611883.
TY - JOUR
T1 - Structure of the Alzheimer's disease amyloid precursor protein copper binding domain. A regulator of neuronal copper homeostasis.
AU - Barnham,Kevin J,
AU - McKinstry,William J,
AU - Multhaup,Gerd,
AU - Galatis,Denise,
AU - Morton,Craig J,
AU - Curtain,Cyril C,
AU - Williamson,Nicholas A,
AU - White,Anthony R,
AU - Hinds,Mark G,
AU - Norton,Raymond S,
AU - Beyreuther,Konrad,
AU - Masters,Colin L,
AU - Parker,Michael W,
AU - Cappai,Roberto,
Y1 - 2003/02/28/
PY - 2003/3/4/pubmed
PY - 2003/7/2/medline
PY - 2003/3/4/entrez
SP - 17401
EP - 7
JF - The Journal of biological chemistry
JO - J Biol Chem
VL - 278
IS - 19
N2 - A major source of free radical production in the brain derives from copper. To prevent metal-mediated oxidative stress, cells have evolved complex metal transport systems. The Alzheimer's disease amyloid precursor protein (APP) is a major regulator of neuronal copper homeostasis. APP knockout mice have elevated copper levels in the cerebral cortex, whereas APP-overexpressing transgenic mice have reduced brain copper levels. Importantly, copper binding to APP can greatly reduce amyloid beta production in vitro. To understand this interaction at the molecular level we solved the structure of the APP copper binding domain (CuBD) and found that it contains a novel copper binding site that favors Cu(I) coordination. The surface location of this site, structural homology of CuBD to copper chaperones, and the role of APP in neuronal copper homeostasis are consistent with the CuBD acting as a neuronal metallotransporter.
SN - 0021-9258
UR - https://www.unboundmedicine.com/medline/citation/12611883/Structure_of_the_Alzheimer's_disease_amyloid_precursor_protein_copper_binding_domain__A_regulator_of_neuronal_copper_homeostasis_
L2 - http://www.jbc.org/cgi/pmidlookup?view=long&pmid=12611883
DB - PRIME
DP - Unbound Medicine
ER -