
<ArticleTitle>A refined structure of human <prot>aquaporin-1</prot>.</ArticleTitle>
<AbstractText>A refined structure of the human water channel <prot>aquaporin-1</prot> is presented. The model rests on the high resolution X-ray structure of the homologous bacterial glycerol transporter <prot>GlpF</prot>, 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 <prot>aquaporin-1</prot> structure. Comparison with previous <prot>aquaporin-1</prot> models shows significant differences, not only in the loop regions, but also in the core of the water channel.</AbstractText>
