Structure-function analysis of plant aquaporin AtPIP2;1 gating by divalent cations and protons.

@article{Verdoucq2008StructurefunctionAO,
  title={Structure-function analysis of plant aquaporin AtPIP2;1 gating by divalent cations and protons.},
  author={Lionel Verdoucq and Alexandre Grondin and Christophe Maurel},
  journal={The Biochemical journal},
  year={2008},
  volume={415 3},
  pages={409-16}
}
Water channel proteins, AQPs (aquaporins), of the PIP (plasma membrane intrinsic protein) subfamily, provide a means for fine and quick adjustments of the plant water status. A molecular model for gating of PIPs by cytosolic protons (H(+)) and divalent cations was derived from the atomic structure of spinach SoPIP2;1 (Spinacia oleracea PIP2;1) in an open- and a closed-pore conformation. In the present study, we produced the Arabidopsis AtPIP2;1 (Arabidopsis thaliana PIP2;1) homologue in Pichia… CONTINUE READING

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