title: Molecular design of aquaporin-1 water channel as revealed by electron crystallography.
abstract: 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.
authors.forename: H
authors.initials: H
authors.lastname: Li
authors.forename: S
authors.initials: S
authors.lastname: Lee
authors.forename: B K
authors.initials: BK
authors.lastname: Jap
mesh_terms: 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
chemical_list: D020346:Aquaporins; D007473:Ion Channels; D014867:Water; D051398:Aquaporin 1