Molecular dynamics study of the Cu2+ binding-induced "structuring" of the N-terminal domain of human prion protein.

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Valensin G, Molteni E, Valensin D, Taraszkiewicz M, Kozlowski H

Molecular dynamics study of the Cu2+ binding-induced "structuring" of the N-terminal domain of human prion protein.

J Phys Chem B. 2009 Mar 19;113(11):3277-9. doi: 10.1021/jp901030a.

PubMed ID

19236027 [ View in PubMed

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Abstract

In this work, we report molecular dynamics simulations on a fragment of the human prion protein spanning residues 31-120, with copper(II) bound to the repeat region in several ways corresponding to the known intra- and inter-repeat coordination modes, or to the metal site located at His111. The results of this study point to a different structuring tendency of the protein fragment depending on copper binding mode, with the highest degree of structuring in the case of intrarepeat Cu(II) coordination corresponding to high copper concentration.

DrugBank Data that Cites this Article

Drug Targets

Drug	Target	Kind	Organism	Pharmacological Action	Actions
Copper	Alternative prion protein	Protein	Humans	Unknown	Not Available	Details