The beta A4 amyloid precursor protein binding to copper.

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Hesse L, Beher D, Masters CL, Multhaup G

The beta A4 amyloid precursor protein binding to copper.

FEBS Lett. 1994 Jul 25;349(1):109-16.

PubMed ID

7913895 [ View in PubMed

]

Abstract

Previously it has been shown that the extracellular domain of transmembrane beta A4 amyloid precursor protein (APP) includes binding sites for zinc(II) and for molecules of the extracellular matrix such as collagen, laminin and the heparin sulfate chains of proteoglycans (HSPGs). Here we report that APP also binds copper ions. A copper type II binding site was located within residues 135-155 of the cysteine-rich domain of APP695 which is present in all eight APP splice isoforms known so far. The two essential histidines in the type II copper binding site of APP are conserved in the related protein APLP2. Copper(II) binding is shown to inhibit homophilic APP binding. The identification of a copper(II) binding site in APP suggests that APP and APLP2 may be involved in electron transfer and radical reactions.

DrugBank Data that Cites this Article

Drug Targets

Drug	Target	Kind	Organism	Pharmacological Action	Actions
Copper	Amyloid beta A4 protein	Protein	Humans	Unknown	Binder	Details

Polypeptides

Name	UniProt ID
Amyloid beta A4 protein	P05067	Details