Abstract
Aquaporin-0 (AQP0) contributes to the nurturing and cleaning of the eye lens of waste product. It is a tetrameric protein composed of four identical monomers, each of which has its own water pore. AQP0 water conduction is regulated by pH, Ca2+ concentration, and the phosphorylation of Serine residues at the C-terminal. High cellular Ca2+ concentration enhances the binding of Calmodulin (CaM), a Ca2+ dependent protein, to AQP0 from cytoplasm. Molecular Dynamics (MD) simulations performed to investigate the effects of two Calmodulin binding to AQP0 tetramer revealed free energy barriers up to 6 kcal/mol for water conduction. MD simulations also exposed three distinct locations, where the water molecule's pathway changes between AQP0-CaM model versus AQP0 open model.
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