In Silico Analysis of Protein–Protein Interactions Between Estrogen Receptor and Fungal Laccase

Abstract

Protein–protein interactions mediate important cellular functions and can act as intervention targets. Estrogen receptors play a vital role in the initiation and progression of breast cancer. The present study was carried out to understand the interactions of the estrogen receptor with laccase, a protein known to have anticancer activity against breast cancer cell lines. The available structures of laccase and estrogen receptors were docked using protein–protein interaction programs, ClusPro (2.0) and pyDock. It was observed that estrogen receptor beta (5TOA) and laccase (IGYC) showed the best binding energy of −43.934 kcal/mol. The complex was further refined using FireDock and subjected to interaction using PDBsum in order to understand the interactions at the molecular level. The proteins were interacting via 6 hydrogen bonds and 164 non-bonded interactions. Some important interacting residues spotted were Arg501, His498, Glu493, Leu324, Gln327 and Lys314 from the estrogen receptor (5TOA) and Ala178, Thr267, Glu392, Arg157 and Leu158 from laccase protein (1GYC).