title: A numerical investigation into possible mechanisms by that the A629P mutant of ATP7A causes Menkes Disease.
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.
authors: Department of Physics, Michigan Technological University, Houghton, MI 49931, USA. mkouza@mtu.edu
authors: Maksim
authors: M
authors: Kouza
authors: S
authors: S
authors: Gowtham
authors: Max
authors: M
authors: Seel
authors: Ulrich H E
authors: UH
authors: Hansmann
mesh_terms: D000251:Adenosine Triphosphatases / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D027682:Cation Transport Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D003300:Copper / Q000378:metabolism; D000073840:Copper-Transporting ATPases; D006801:Humans; D007706:Menkes Kinky Hair Syndrome / Q000235:genetics* / Q000378:metabolism; D008958:Models, Molecular; D009154:Mutation; D019906:Nuclear Magnetic Resonance, Biomolecular; D011485:Protein Binding; D017433:Protein Structure, Secondary
chemical_list: D027682:Cation Transport Proteins; D003300:Copper; D000251:Adenosine Triphosphatases; C081184:ATP7A protein, human; D000073840:Copper-Transporting ATPases