INTERNATIONAL JOURNAL OF PURE & APPLIED BIOSCIENCE

ISSN : 2320-7051

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International Journal of Pure & Applied Bioscience (IJPAB)
Year : 2019, Volume : 7, Issue : 3
First page : (269) Last page : (277)
Article doi: : http://dx.doi.org/10.18782/2320-7051.7558

Studies on 3D Structure Prediction and Binding Modes of Kisspeptin Receptor 1 Complexed with Kisspeptin 1 using
Molecular Docking Approach

Riya Kumari1*, Mukesh Kumar1, Gulshan Kumar1 and Sujit Kumar2

1Department of Fish Genetics and Biotechnology,
ICAR-Central Institute of Fisheries Education, Versova, Mumbai, India -400061
2PGIFER, Kamdhenu University, Gandhinagar, Gujarat
*Corresponding Author E-mail: riya.fgbpa701@cife.edu.in
Received: 15.02.2019  |  Revised: 27.03.2019   |  Accepted: 6.04.2019  

 

 ABSTRACT

Kisspeptin (Kiss), a neuropeptide belongs to the RF-amide peptide family which activates the kisspeptin receptor at puberty. Kisspeptin is recognized as an upstream regulator of reproductive events in teleost. The popular food and game fish golden mahseer (Tor putitora) is an important aquaculture species in recent years due to high market demand. kisspeptin1 and its receptor modulation is a significantly important event during early development and gonadal sex maturation. The present study was aimed to characterize the kisspeptin1 and its receptor from human, mouse, fish (Tor putitora) and also to identify the binding mode of kisspeptin1 and its receptor. The tertiary structure of Kiss1r was developed using the Swiss model server. The best model was selected based upon the Ramachandran plot and Errat server. Molecular docking method was applied to identify the binding modes between Kiss1r and Kiss1 using ZDOCK server. The physicochemical properties revealed that the kisspeptin and its receptor is basic in nature, unstable, lower extinction coefficient in case of kiss1 but higher in case of kiss1r. kisspeptin1 is hydrophilic in nature whereas kisspeptin1r is hydrophobic in nature. The functional properties showed that kisspeptin1 had no transmembrane helix whereas kisspeptin1 receptor was composed of seven transmembrane helices. The secondary structure revealed the dominance of random coils followed by the alpha helix, extended strands and beta turns in kisspeptin1 whereas, alpha helix dominated followed by the random coils, extended strands and beta turns for the kisspeptin1r. The docking study revealed the highest binding energy between Kiss1r and Kiss1.

Key words: Kisspeptin, Molecular docking, Ramachandran plot and Errat server

Full Text : PDF; Journal doi : http://dx.doi.org/10.18782

Cite this article: Kumari, R., Kumar, M., Kumar, G., Kumar, S., Studies on 3D Structure Prediction and Binding Modes of Kisspeptin Receptor 1 Complexed with Kisspeptin 1 using Molecular Docking Approach, Int. J. Pure App. Biosci.7(3): 269-277 (2019). doi: http://dx.doi.org/10.18782/2320-7051.7558




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