Molecular dynamics insights into human aquaporin 2 water channel.
In this study, the first molecular dynamics simulation of the human aquaporin 2 is performed and for a better understanding of the aquaporin 2 permeability performance, the characteristics of water transport in this protein channel and key biophysical parameters of AQP2 tetramer including osmotic and diffusive permeability constants and the pore radius are investigated. For this purpose, recently recovered high resolution X-ray crystal structure of` the human aquaporin 2 is used to perform twenty nanosecond molecular dynamics simulation of fully hydrated tetramer of this protein embedded in a lipid bilayer. The resulting water permeability characteristics of this protein channel showed that the water permeability of the human AQP2 is in a mean range in comparison with other human aquaporins family. Finally, the results reported in this research demonstrate that molecular dynamics simulation of human AQP2 provided useful insights into the mechanisms of water permeation and urine concentration in the human kidney.
School of Mechanical Engineering, Shiraz University, Shiraz 71348-51154, Iran. Electronic address: binesh@shirazu.ac.ir.
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Binesh
School of Mechanical Engineering, Shiraz University, Shiraz 71348-51154, Iran. Electronic address: rkamali@shirazu.ac.ir.
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Kamali
D051399:Aquaporin 2 / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D008051:Lipid Bilayers / Q000737:chemistry / Q000378:metabolism; D056004:Molecular Dynamics Simulation; D010539:Permeability; D014867:Water / Q000737:chemistry* / Q000378:metabolism
D051399:Aquaporin 2; D008051:Lipid Bilayers; D014867:Water
Aquaporin; Molecular dynamics; Nephrogenic diabetes insipidus; Water permeation