A refined structure of human aquaporin‐1

FEBS Letters

Grubmüller, Helmut¹  Engel, Andreas²  de Groot, Bert L.¹ 

[1]Max Planck Institute for Biophysical Chemistry, Theoretical Molecular Biophysics Group, Am Fassberg 11, 37077 Göttingen, Germany

[2]M.E. Müller Institute for Microscopic Structural Biology, Biozentrum, University of Basel, CH-4056 Basel, Switzerland

关键词: Protein structure;    Electron microscopy;    Water transport;    Water channel;    Membrane protein;    Glycerol transporter;    Aquaporin-1;    GlpF;   

DOI  :  10.1016/S0014-5793(01)02743-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown