5J0Z
Crystal structure of GLIC in complex with DHA
Summary for 5J0Z
| Entry DOI | 10.2210/pdb5j0z/pdb |
| Descriptor | Proton-gated ion channel, CHLORIDE ION, DODECYL-BETA-D-MALTOSIDE, ... (8 entities in total) |
| Functional Keywords | plgic, cys loop, glic, membrane protein |
| Biological source | Gloeobacter violaceus (strain PCC 7421) |
| Total number of polymer chains | 5 |
| Total formula weight | 184340.00 |
| Authors | Basak, S.,Schmandt, N.,Chakrapani, S. (deposition date: 2016-03-28, release date: 2017-03-15, Last modification date: 2023-09-27) |
| Primary citation | Basak, S.,Schmandt, N.,Gicheru, Y.,Chakrapani, S. Crystal structure and dynamics of a lipid-induced potential desensitized-state of a pentameric ligand-gated channel. Elife, 6:-, 2017 Cited by PubMed Abstract: Desensitization in pentameric ligand-gated ion channels plays an important role in regulating neuronal excitability. Here, we show that docosahexaenoic acid (DHA), a key ω-3 polyunsaturated fatty acid in synaptic membranes, enhances the agonist-induced transition to the desensitized state in the prokaryotic channel GLIC. We determined a 3.25 Å crystal structure of the GLIC-DHA complex in a potentially desensitized conformation. The DHA molecule is bound at the channel-periphery near the M4 helix and exerts a long-range allosteric effect on the pore across domain-interfaces. In this previously unobserved conformation, the extracellular-half of the pore-lining M2 is splayed open, reminiscent of the open conformation, while the intracellular-half is constricted, leading to a loss of both water and permeant ions. These findings, in combination with spin-labeling/EPR spectroscopic measurements in reconstituted-membranes, provide novel mechanistic details of desensitization in pentameric channels. PubMed: 28262093DOI: 10.7554/eLife.23886 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.25 Å) |
Structure validation
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