Human aryl-hydrocarbon receptor and its interaction with dioxin and physiological ligands investigated by molecular modelling and docking simulations

Maria Salzano, Anna Marabotti, Luciano Milanesi, Angelo Facchiano

Research output: Contribution to journalArticlepeer-review

Abstract

Molecular structure of the ligand binding domain of hAhR has been modelled by homology modelling techniques and used for docking simulations with dioxin and nine more xenobiotics and endogenous ligands. The study evidences that different sites may bind these ligands, whereas only one binding site has been previously indicated by past studies on the mouse homologous receptor. The differences in the sequence of mouse and human AhR ligand binding domain may explain this observation, being most of them in the additional sites observed. Preferences of the evaluated ligands for the different sites are reported and discussed in view of their functional role.

Original languageEnglish
Pages (from-to)176-181
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume413
Issue number2
DOIs
Publication statusPublished - Sep 23 2011

Keywords

  • Aryl-hydrocarbon receptor
  • Dioxin
  • Docking simulations
  • Xenobiotics

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Cell Biology
  • Molecular Biology

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