Molecular design of aquaporin-1 water channel as revealed by electron crystallography.
The electron crystallographic structure of the aquaporin-1 water channel, determined at approximately 6A, reveals that the protein has six transmembrane alpha-helices forming a trapezoid-like cylinder. There is a branched rod-like structure within the cylinder that traverses the membrane and likely contains at least one alpha-helix.
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D051398:Aquaporin 1; D020346:Aquaporins; D001692:Biological Transport; D003461:Crystallography; D004583:Electrons; D007473:Ion Channels / Q000737:chemistry*; D008958:Models, Molecular; D011487:Protein Conformation; D014867:Water / Q000378:metabolism
D020346:Aquaporins; D007473:Ion Channels; D014867:Water; D051398:Aquaporin 1