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Issue 37, 2010
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A numerical investigation into possible mechanisms by that the A629P mutant of ATP7A causes Menkes Disease

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Abstract

We study in silico possible mechanisms by that the A629P mutant of ATP7A causes Menkes Disease. Our results indicate that the mutation does not have appreciable affects on the stability of copper-bound states but rather destabilizes the characteristic end-to-end β-sheet. In this way, the mutation presumably increases the probability for aggregation and/or degradation leading to decreased concentration of the monomer.

Graphical abstract: A numerical investigation into possible mechanisms by that the A629P mutant of ATP7A causes Menkes Disease

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Article information


Submitted
23 Feb 2010
Accepted
14 Jun 2010
First published
16 Aug 2010

Phys. Chem. Chem. Phys., 2010,12, 11390-11397
Article type
Paper

A numerical investigation into possible mechanisms by that the A629P mutant of ATP7A causes Menkes Disease

M. Kouza, S. Gowtham, M. Seel and U. H. E. Hansmann, Phys. Chem. Chem. Phys., 2010, 12, 11390 DOI: 10.1039/C003568H

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