alexa Homology Modeling and Structural Analysis of NHX Antiporter of Leptochloa fusca (L.)
ISSN: 0974-276X

Journal of Proteomics & Bioinformatics
Open Access

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Research Article

Homology Modeling and Structural Analysis of NHX Antiporter of Leptochloa fusca (L.)

Bahman Panahi1*, Nasrin Moshtaghi1, Ibrahim Torktaz2, Askar panahi3 and Sudeep Roy4

1Department of Biotechnology and Plant Breeding, Ferdowsi University of Mashhad, Mashhad, Iran

2Department of Biotechnology, University of Isfahan, Iran

3Department of Biology, University of Mohaghegh Ardabili, Iran

4Biotechnology Division, Central Institute of Medicinal and Aromatic Plants, India

*Corresponding Author:
Bahman Panahi
Department of Biotechnology and Plant Breeding
Ferdowsi University of Mashhad, Mashhad, Iran
E-mail: [email protected]

Received Date: August 17, 2012; Accepted Date: September 10, 2012; Published Date: September 10, 2012

Citation: Panahi B, Moshtaghi N, Torktaz I, panahi A, Roy S (2012) Homology Modeling and Structural Analysis of NHX Antiporter of Leptochloa fusca (L.). J Proteomics Bioinform 5: 214-216. doi: 10.4172/jpb.1000238

Copyright: © 2012 Panahi B, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

 

Abstract

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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