9SHE
Structure of the honeybee GABAA RDL receptor with GABA and Abamectin
This is a non-PDB format compatible entry.
Summary for 9SHE
| Entry DOI | 10.2210/pdb9she/pdb |
| EMDB information | 54897 |
| Descriptor | Gamma-aminobutyric acid receptor subunit beta, GAMMA-AMINO-BUTANOIC ACID, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total) |
| Functional Keywords | gabaa receptor, insect, neurotransmission, insecticides, membrane protein |
| Biological source | Apis mellifera (honey bee) |
| Total number of polymer chains | 5 |
| Total formula weight | 274680.29 |
| Authors | |
| Primary citation | Laboure, T.,Pandey, M.P.,Zarkadas, E.,Juillan-Binard, C.,Baud, D.,Neyton, J.,Cens, T.,Rousset, M.,Dehez, F.,Charnet, P.,Nury, H. Structures of the honeybee GABA A RDL receptor illuminate allosteric modulation. Neuron, 2026 Cited by PubMed Abstract: A large share of insecticides targets insect ion channels. In particular, the GABA RDL (resistant to dieldrin) receptor is targeted by old pore blockers or more recent allosteric modulators binding to a cavity of its transmembrane domain. Here, we describe three ligand-binding sites and the associated receptor conformations, using a combination of cryoelectron microscopy (cryo-EM), electrophysiology, and molecular dynamics. The GABA site geometry is well conserved with that of mammalian receptors, in line with the absence of orthosteric insecticide. The transmembrane modulation site, occupied here by abamectin, exists in a closed-pore conformation. We identify a second allosteric transmembrane site using a compound named chrodrimanin B. Structures also reveal the existence of a conformation-dependent PIP lipid site. We anticipate our results to be the starting point for investigations on the physiological modulation of insect GABA receptors. The honeybee receptor structures may also foster the search for species-specific, environmentally benign insecticides. PubMed: 41653930DOI: 10.1016/j.neuron.2025.12.013 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.2 Å) |
Structure validation
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