Journal
FEBS LETTERS
Volume 579, Issue 24, Pages 5287-5292Publisher
WILEY
DOI: 10.1016/j.febslet.2005.08.052
Keywords
Hah1; copper(I); molecular dynamics; metal-binding site
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Molecular dynamics simulations were performed on both apo and copper forms of the human copper chaperone, Hah1. Wild-type Hah1 and a methionine (M10) to serine mutant were investigated. We have evidenced the central role of residue M10 in stabilizing the hydrophobic core of Hah1 as well as the internal structure of the metal-binding site. When copper(l) is bound, the mobility of Hah1 is reduced whereas mutation of M10 implies a drastic increase of the mobility of apoHah1, stressing the importance of this highly conserved hydrophobic residue for copper sequestration by the apoprotein. (c) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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