Eric A. Zizzi
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Taste receptors and food molecules

The structure and dynamics of bitter taste receptors such as TAS2R46, and computational tools that predict which molecules they recognise.

Bitter taste receptors (TAS2Rs) are proteins that detect bitter compounds, in the mouth and in many other tissues. They are hard to study experimentally, which makes them a good fit for computational methods.

I have studied the internal mechanics of the bitter receptor TAS2R46 with molecular dynamics and network analysis, and I work with colleagues on tools that predict which molecules a receptor will recognise, from structure-based screening of protein–ligand complexes to explainable machine-learning models. Much of this work grew out of the EU project VIRTUOUS.

Line drawing of the TAS2R46 receptor backbone with strychnine in its binding pocket; 6 measured contacts are listed below the figure.≤ 4.0 Å1Asn653.0 Å2Tyr853.1 Å3Glu2653.2 Å4Trp883.3 Å5Thr1803.4 Å6Leu623.5 Å

The human bitter taste receptor TAS2R46 holding strychnine. I study how this receptor moves, and help build models that predict which molecules bitter receptors recognise.

Marked: every residue with a heavy atom within 4.0 Å of strychnine, with the shortest distance, measured from the deposited coordinates.

Structure: PDB 7XP6 (Xu et al., Science 2022)

Receptor–strychnine contacts within 4.0 Å
#ResidueAtoms (receptor – ligand)Distance
1Asn65OD1 – CAC3.0 Å
2Tyr85CD1 – OAJ3.1 Å
3Glu265OE2 – NAY3.2 Å
4Trp88CG – CAE3.3 Å
5Thr180OG1 – OAO3.4 Å
6Leu62CD1 – CAC3.5 Å

Papers on this theme

Projects on this theme

  • VIRTUOUS