Eukaryotic NHX transporters are trans-membrane proteins which are vital for cellular homeostasis. Plants vacuolar NHX antiporters have been suggested to be involved in sequestering Na+ into vacuoles, thus preventing toxic effects of Na+ in the cytoplasm. Primary and secondary structure analysis of NHX antiporter of Leptochloa fusca suggested that this antiporter is a hydrophobic protein containing a significant proportion of alpha helixes. In this study, a three-dimensional structures of NHX antiporter predicted by in silico 3D homology modeling studies. The resulting model was refined by energy minimization, subjected to the quality assessment from both geometric and energetic aspects and was found to be of reasonable quality. Validation of 3D structure was done by plotting Ramachandran plot and calculation of QMEAN score. This predicted information will help in better understanding of mechanisms underlying to salt tolerance in monocot plants and use of this information in protein engineering to improve plants to high salinity conditions.

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