A molecular modeling approach defines a new group of Nodulin 26-like aquaporins in plants
- Surfaces Cellulaires et Signalisation chez les Vegetaux, UMR Universite Paul Sabatier-CNRS 5546, 24 Chemin de Borde Rouge, 31326 Castanet Tolosan (France)
The three-dimensional models built for the Nod26-like aquaporins all exhibit the typical {alpha}-helical fold of other aquaporins containing the two ar/R and NPA constriction filters along the central water channel. Besides these structural homologies, they readily differ with respect to the amino acid residues forming the ar/R selective filter. According to these discrepancies in both the hydrophilicity and pore size of the ar/R filter, Nod26-like aquaporins can be distributed in three subgroups corresponding to NIP-1, NIP-II and a third subgroup of Nod26-like aquaporins exhibiting a highly hydrophilic and widely open filter. However, all Nod26-like aquaporins display a bipartite distribution of electrostatic charges along the water channel with an electropositive extracellular vestibular portion followed by an electronegative cytosolic vestibular portion. The specific transport of water, non-ionic solutes (glycerol, urea, ammoniac), ions (NH{sub 4}{sup +}) and gas (NH{sub 3}) across the Nod26-like obviously depends on the electrostatic and conformational properties of their central water channel.
- OSTI ID:
- 21043634
- Journal Information:
- Biochemical and Biophysical Research Communications, Vol. 367, Issue 1; Other Information: DOI: 10.1016/j.bbrc.2007.12.079; PII: S0006-291X(07)02710-6; Copyright (c) 2007 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA); ISSN 0006-291X
- Country of Publication:
- United States
- Language:
- English
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