How broadly tuned olfactory receptors equally recognize their agonists. Human OR1G1 as a test case

Cell Mol Life Sci. 2012 Dec;69(24):4205-13. doi: 10.1007/s00018-012-1116-0. Epub 2012 Aug 29.


The molecular features that dominate the binding mode of agonists by a broadly tuned olfactory receptor are analyzed through a joint approach combining cell biology, calcium imaging, and molecular modeling. The odorant/receptor affinities, estimated through statistics accrued during molecular dynamics simulations, are in accordance with the experimental ranking. Although in many systems receptors recognize their target through a network of oriented interactions, such as H-bonding, the binding by broadly tuned olfactory receptors is dominated by non-polar terms. We show how such a feature allows chemicals belonging to different chemical families to similarly activate the receptors through compensations of interactions within the binding site.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Binding Sites
  • Calcium / metabolism
  • HEK293 Cells
  • Humans
  • Ligands
  • Models, Biological
  • Protein Structure, Tertiary
  • Receptors, Odorant / chemistry
  • Receptors, Odorant / metabolism
  • Receptors, Odorant / physiology*
  • Smell / physiology


  • Ligands
  • OR1G1 protein, human
  • Receptors, Odorant
  • Calcium