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FEBS Lett. 2001 Aug 31;504(3):206-11.

A refined structure of human aquaporin-1.

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  • 1Max Planck Institute for Biophysical Chemistry, Theoretical Molecular Biophysics Group, G├Âttingen, Germany.


A refined structure of the human water channel aquaporin-1 is presented. The model rests on the high resolution X-ray structure of the homologous bacterial glycerol transporter GlpF, electron crystallographic data at 3.8 A resolution and a multiple sequence alignment of the aquaporin superfamily. The crystallographic R and free R values (36.7% and 37.8%) for the refined structure are significantly lower than for previous models. Improved geometry and enhanced stability in molecular dynamics simulations demonstrate a significant improvement of the aquaporin-1 structure. Comparison with previous aquaporin-1 models shows significant differences, not only in the loop regions, but also in the core of the water channel.

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