A refined structure of human aquaporin-1

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. Th...

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Bibliographic Details
Published in:FEBS letters 2001-08, Vol.504 (3), p.206-211
Main Authors: de Groot, Bert L., Engel, Andreas, Grubmüller, Helmut
Format: Article
Language:English
Subjects:
Aquaporin 1
Aquaporins - chemistry
Bacterial Outer Membrane Proteins - chemistry
Blood Group Antigens
Cell Membrane - chemistry
Computer Simulation
Crystallography, X-Ray
Electron microscopy
Electrons
Escherichia coli Proteins
GlpF
Glycerol transporter
Humans
Membrane protein
Microscopy, Electron
Models, Molecular
Protein Conformation
Protein structure
Protein Structure, Tertiary
Water - chemistry
Water channel
Water transport
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Summary: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.
ISSN:0014-5793
1873-3468
DOI:10.1016/S0014-5793(01)02743-0