<i style="mso-bidi-font-style:normal">In silico</i> analysis of the structure and interaction of COP1 protein of <i style="mso-bidi-font-style:normal">Arabidopsis thaliana</i>

Abstract

Previous studies have shown that COP1 (constitutive photomorphogenic 1) protein of <i style="mso-bidi-font-style:normal">Arabidopsis thaliana</i> plays a crucial role in different aspects of photomorphogenesis. Interaction of COP1 with SPA1 (suppressor of phytochrome A)and other regulatory proteins actively affect light regulatory gene expression in diverse directions. Though several studies have explained the function of COP1 protein, method of its interaction with SPA1 and cryptochromes are still not explained in detail. In this study, <i style="mso-bidi-font-style:normal">in silico</i> analysis was followed to predict the tertiary structure, active site residues, functionally important regions and regular expressions of COP1 protein. Its ease of its interaction with SPA1 and seven other regulatory proteins, namely bZIP transcription factor 56 (HY5), transcription factor HY5-like (HYH), serine/threonine-protein phosphatase 7 (AtPP7), protein long hypocotyl in FAR-RED 1 (HFR1), OBP3-responsive protein 1 (OBP3), transcription factor MYC2 (MYC2/ZBF1) and Z-box binding factor 2 protein (GBF1/ZBF2) was measured using protein-protein docking. Interaction with MYC2 was found to be stronger than with others with a global energy value of -22.46. It was also found that COP1 shared three regions of regular expression with SPA1, the last expression also being present in MYC2/ZBF1 and OBP3. Taken together, the insight into structural and functional properties of COP1 protein presented in this study would be helpful in determining the role of COP1 in unknown mechanisms of photomorphogenesis.