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Published March 2015 | metadata_only
Journal Article

Deciphering the odorant binding protein - olfactory receptor interactions


Olfactory receptors (OR) belong to the family of GPCR and participate to the recognition of odorants. Prior to the activation of the OR, odorants are disolved in the olfactory mucus by odorant binding proteins (OBP). Belonging to the family of lipocalins, they are small carrier proteins and are considered as non-specific binders. OBP would contribute to the olfaction process by carrying hydrophobic odorant molecules to the OR. Due to the transmembrane nature of these receptors, it remains a hard task to obtain their crystal structure. Molecular modeling methods are perfectly suited to provide relevant three-dimensional models of unknown structures to further gain insights on the structural features of protein-protein complexes. Molecular models of hOR2T4 and rORI7 have been built using both ab initio homology modeling approaches. To understand how OBPs release odorants and participate to the modulation of OR activation, state of the art protein-protein docking [4] have been performed to predict OR-OBP complexes structure (Figure 1). We propose models of interactions showing how rOBP3 is connected to the extracellular loop 2 of hORI7. To decipher the underlying molecular mechanism, molecular dynamics simulations have been carried out to estimate the octanal-rOBP3 free energy of binding. The formation of the OBP-OR complex destabilizes the odorant-OBP interactions prior to the release of the odorant.

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© 2015 Oxford University Press.

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August 20, 2023
August 20, 2023