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Structure of an insect gustatory receptor.

bioRxiv : the preprint server for biology | 2023

Gustatory Receptors (GRs) are critical for insect chemosensation and are potential targets for controlling pests and disease vectors. However, GR structures have not been experimentally determined. We present structures of Bombyx mori Gr9 (BmGr9), a fructose-gated cation channel, in agonist-free and fructose-bound states. BmGr9 forms a tetramer similar to distantly related insect Olfactory Receptors (ORs). Upon fructose binding, BmGr9's ion channel gate opens through helix S7b movements. In contrast to ORs, BmGR9's ligand-binding pocket, shaped by a kinked helix S4 and a shorter extracellular S3-S4 loop, is larger and solvent accessible in both agonist-free and fructose-bound states. Also unlike ORs, fructose binding by BmGr9 involves helix S5 and a binding pocket lined with aromatic and polar residues. Structure-based sequence alignments reveal distinct patterns of ligand-binding pocket residue conservation in GR subfamilies associated with distinct ligand classes. These data provide insight into the molecular basis of GR ligand specificity and function.

Pubmed ID: 38187590 RIS Download

Research resources used in this publication

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Associated grants

  • Agency: NIAID NIH HHS, United States
    Id: R01 AI157194
  • Agency: NIGMS NIH HHS, United States
    Id: R01 GM096053
  • Agency: NIGMS NIH HHS, United States
    Id: R01 GM120996
  • Agency: NIDCD NIH HHS, United States
    Id: R21 DC018497

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