Copper-transfer mechanism from the human chaperone Atox1 to a metal-binding domain of wilson disease protein

The molecular details of how copper (Cu) is transferred from the human Cu chaperone Atox1 to metalbinding domains (MBDs) of P1B-type ATPases are still unclear. Here, we use a computational approach, employing quantum mechanics/molecular mechanics (QM/MM) methods, to shed light on the reaction mechan...

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Detalles Bibliográficos
Autores principales: Rodriguez-Granillo, A., Crespo, A., Estrin, D.A., Wittung-Stafshede, P.
Formato: JOUR
Materias:
Coordination reactions
Activation barriers
ATPases
Computational approach
Coordination geometry
Cys residues
Experimental data
Intermediate specie
Metal binding domain
Metal-binding motif
Molecular mechanism
Reaction mechanism
Reaction paths
Secretory pathways
Transfer mechanisms
Transfer reaction
Wilson disease
Reaction intermediates
adenosine triphosphatase
ATOX1 protein, human
cation transport protein
chaperone
copper
metal
Wilson disease protein
article
chemistry
human
metabolism
molecular dynamics
protein binding
protein tertiary structure
quantum theory
thermodynamics
Adenosine Triphosphatases
Cation Transport Proteins
Copper
Humans
Metals
Molecular Chaperones
Molecular Dynamics Simulation
Protein Binding
Protein Structure, Tertiary
Quantum Theory
Thermodynamics
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_15206106_v114_n10_p3698_RodriguezGranillo
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

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