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 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 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.
de Groot
B L
BL
Max Planck Institute for Biophysical Chemistry, Theoretical Molecular Biophysics Group, Göttingen, Germany.
Engel
A
A
Grubmüller
H
H
D051398:Aquaporin 1; D020346:Aquaporins / Q000737:chemistry*; D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry; D001789:Blood Group Antigens; D002462:Cell Membrane / Q000737:chemistry; D003198:Computer Simulation; D018360:Crystallography, X-Ray; D004583:Electrons; D029968:Escherichia coli Proteins; D006801:Humans; D008854:Microscopy, Electron; D008958:Models, Molecular; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D014867:Water / Q000737:chemistry
C496020:AQP1 protein, human; D020346:Aquaporins; D001425:Bacterial Outer Membrane Proteins; D001789:Blood Group Antigens; D029968:Escherichia coli Proteins; D014867:Water; C078043:GlpF protein, E coli; D051398:Aquaporin 1