10.5452/MA-AJFZ7
Ampah-Korsah, Henry; Sonntag, Yonathan; Engfors, Angelica; Kirscht, Andreas; Kjellbom, Per; Johanson, Urban
Single amino acid substitutions in the selectivity filter render NbXIP1;1α aquaporin water permeable - Mutant 6
modelarchive.org
2017
3D macromolecular model
2017-02-03
en
Aquaporins (AQPs) are integral membrane proteins that facilitate transport of water and/or other small neutral solutes across membranes in all forms of life. The X Intrinsic Proteins (XIPs) are the most recently recognized and the least characterized aquaporin subfamily in higher plants. XIP1s have been shown to be impermeable to water but permeable to boric acid, glycerol, hydrogen peroxide and urea. However, uncertainty of the determinants for selectivity and lack of an activity that is easy to quantify in spheroplasts, have hindered functional investigations. In an effort to resolve these issues, we set out to introduce water permeability in Nicotiana benthamiana NbXIP1;1α (NbXIP1;1α), by exchanging predicted alternative aromatic/arginine (ar/R) selectivity filters of NbXIP1;1α for the water permeable ar/R selectivity filter of AtTIP2;1.