[HTML][HTML] A refined structure of human aquaporin-1

BL de Groot, A Engel, H Grubmüller - Febs Letters, 2001 - Elsevier
Febs Letters, 2001Elsevier
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 Ċ 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 …
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 Ċ 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.
Elsevier