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

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 pr...

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Bibliographic Details
Published in:Physical chemistry chemical physics : PCCP 2010-01, Vol.12 (37), p.11390-11397
Main Authors: KOUZA, Maksim, GOWTHAM, S, SEEL, Max, HANSMANN, Ulrich H. E
Format: Article
Language:English
Subjects:
Adenosine Triphosphatases - chemistry
Adenosine Triphosphatases - genetics
Adenosine Triphosphatases - metabolism
Cation Transport Proteins - chemistry
Cation Transport Proteins - genetics
Cation Transport Proteins - metabolism
Chemistry
Copper - metabolism
Copper-transporting ATPases
Exact sciences and technology
General and physical chemistry
Humans
Menkes Kinky Hair Syndrome - genetics
Menkes Kinky Hair Syndrome - metabolism
Models, Molecular
Mutation
Nuclear Magnetic Resonance, Biomolecular
Protein Binding
Protein Structure, Secondary
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Summary: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.
ISSN:1463-9076
1463-9084
DOI:10.1039/c003568h