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  A refined structure of human Aquaporin 1.

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

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0012-F5D4-F Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-E289-6
Genre: Journal Article

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 Creators:
de Groot, B. L.1, Author              
Engel, A., Author
Grubmueller, H.1, Author              
Affiliations:
1Research Group of Theoretical Molecular Biophysics, MPI for biophysical chemistry, Max Planck Society, ou_578630              

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 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.

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Language(s): eng - English
 Dates: 2001
 Publication Status: Published in print
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 Identifiers: eDoc: 224287
Other: 34838
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Title: FEBS Letters
Source Genre: Journal
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Pages: - Volume / Issue: 504 (3) Sequence Number: - Start / End Page: 206 - 211 Identifier: -