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SUMoylation is a posttranslational modification occurring to a number of cellular proteins which play key
roles in cellular process. This process is transient, highly regulated and is essential for normal function of
cell.
Cyclodiene are the most potent family of pesticides. Residual contamination of this family of pesticides
has been reported from all over the world. They are highly stable and persistent in the environment for
decades. Uptake of humans leads to accumulation of these pesticides or their metabolites in tissues,
mainly in adipose tissue. Evidently, this leads to neurological disorders, endocrine disruption and cancer.
Noncovalent interaction between Ubc9 and SUMO support SUMO chain formation In the present study
the Cyclodienes were docked insilico to identify possible interaction with human SUMo1 and UBC9
(SUMoylation pathway enzyme, E2) by employing three different docking tools. The results were
visualized in PyMol and 2D representations of the protein- ligand complexes were generated in
LIGPLOT. Potential ligand binding pockets were generated for SUMO1 and UBC9 by MetaPocket2.0.
Endosulfan and, Endosulfansulfate show polar interactions at Asp 73 and Arg 70of SUMo1 (in addition
non-polar interactions at lys48, pro58, Arg63, Phe 64, Ile 71 and Ala 72). The amino acids that
contributed to the binding are represented in the potential binding pocket generated by Metapocket 2.0.
Besides, Heptachlor, HEOM and Chlordan(which are structurally related to endosulfan) also show
interaction at Arg 70.If proved experimentally, this interaction of SUMO1 at Arg 70 is noteworthy as this
amino acid is required for association with E1 enzyme in SUMoylation process.
Endosulfan and, Endosulfansulfate show polar interactions at Ala 26 and Trp 16and non-polar
interactionsat Thr 91, Glu 98, Arg 17, Lys 74 & Cys 93 of UBC9.
Keywords: Cyclodienes; Docking; SUMo; UBC9.