In-Silico Analysis of Structural and Functional Aspects of Salt Responsive Protein of SKP-1 Like Protein 1A

Author(s): G. Anbarasi*, M. P. Arulmoorthy and R. Suresh

Abstract: Abiotic stresses limiting plant growth and productivity. By modulating the amount and activity of regulatory proteins, ubiquitination plays a central role in regulating the transcriptional changes required for adaption to abiotic stresses. S-phase kinase-associated protein 1 (SKP1) is a component of a Skp1-Cullin1-F-box (SCF) complex that facilitates ubiquitin-mediated protein degradation in stress-related signaling and response mechanism. The present study has been carried out to predict the structure and function of a salt responsive protein of SKP1-like protein1A. The uncharacterized protein analyzed in the present study showed conserved domain characteristics of sequence resembles S-phase kinase-associated protein 1 (SKP1) family. The protein exhibited a maximum number of random coils (30.72%)) with alpha helix (63.86%) and extended strands (5.42%)) as secondary structural elements. Three-Dimensional modeling was carried out to elucidate its structure and its active sites. These results aid to the experimental data and help to built up a complete view of SKP1-like protein1A role in plant stress response.

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