title: Water transporters: how so fast yet so selective?
abstract: A high-resolution X-ray structure of an aquaporin has revealed water molecules bound within the transmembrane pore and provided new clues to the mechanisms of rapid water transport and high selectivity in this important class of membrane proteins.
authors.affiliation: Laboratory of Molecular Biophysics, Department of Biochemistry, The University of Oxford, The Rex Richards Building, South Parks Road, OX1 3QU, Oxford, UK.
authors.forename: Richard J
authors.initials: RJ
authors.lastname: Law
authors.forename: Mark S P
authors.initials: MS
authors.lastname: Sansom
mesh_terms: D051398:Aquaporin 1; D020346:Aquaporins / Q000737:chemistry*; D029968:Escherichia coli Proteins / Q000737:chemistry*; D008958:Models, Molecular; D017434:Protein Structure, Tertiary; D014867:Water / Q000737:chemistry*
chemical_list: D020346:Aquaporins; D029968:Escherichia coli Proteins; D014867:Water; C078043:GlpF protein, E coli; D051398:Aquaporin 1