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Journal Article

A refined structure of human Aquaporin 1.

MPS-Authors
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de Groot,  B. L.
Research Group of Theoretical Molecular Biophysics, MPI for biophysical chemistry, Max Planck Society;

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Grubmueller,  H.
Research Group of Theoretical Molecular Biophysics, MPI for biophysical chemistry, Max Planck Society;

Fulltext (public)

599911.pdf
(Publisher version), 976KB

Supplementary Material (public)
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Citation

de Groot, B. L., Engel, A., & Grubmueller, H. (2001). A refined structure of human Aquaporin 1. FEBS Letters, 504(3), 206-211.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0012-F5D4-F
Abstract
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 Å 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.