Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structural basis for cannabinoid-induced potentiation of alpha1-glycine receptors in lipid nanodiscs.
Journal, issue, pages	Nat Commun, Vol. 13, Issue 1, Page 4862, Year 2022
Publish date	Aug 18, 2022
Authors	Arvind Kumar / Kayla Kindig / Shanlin Rao / Afroditi-Maria Zaki / Sandip Basak / Mark S P Sansom / Philip C Biggin / Sudha Chakrapani /
PubMed Abstract	Nociception and motor coordination are critically governed by glycine receptor (GlyR) function at inhibitory synapses. Consequentially, GlyRs are attractive targets in the management of chronic pain ...Nociception and motor coordination are critically governed by glycine receptor (GlyR) function at inhibitory synapses. Consequentially, GlyRs are attractive targets in the management of chronic pain and in the treatment of several neurological disorders. High-resolution mechanistic details of GlyR function and its modulation are just emerging. While it has been known that cannabinoids such as Δ-tetrahydrocannabinol (THC), the principal psychoactive constituent in marijuana, potentiate GlyR in the therapeutically relevant concentration range, the molecular mechanism underlying this effect is still not understood. Here, we present Cryo-EM structures of full-length GlyR reconstituted into lipid nanodisc in complex with THC under varying concentrations of glycine. The GlyR-THC complexes are captured in multiple conformational states that reveal the basis for THC-mediated potentiation, manifested as different extents of opening at the level of the channel pore. Taken together, these structural findings, combined with molecular dynamics simulations and functional analysis, provide insights into the potential THC binding site and the allosteric coupling to the channel pore.
External links	Nat Commun / PubMed:35982060 / PubMed Central
Methods	EM (single particle)
Resolution	2.61 - 3.61 Å
Structure data	23700 7m6m EMDB-23700, PDB-7m6m: Full length alpha1 Glycine receptor in presence of 32uM Tetrahydrocannabinol Method: EM (single particle) / Resolution: 3.09 Å 23701 7m6n EMDB-23701, PDB-7m6n: Full length alpha1 Glycine receptor in presence of 0.1mM Glycine Method: EM (single particle) / Resolution: 2.61 Å 23702 7m6o EMDB-23702, PDB-7m6o: Full length alpha1 Glycine receptor in presence of 0.1mM Glycine and 32uM Tetrahydrocannabinol Method: EM (single particle) / Resolution: 2.84 Å 23703 7m6p EMDB-23703, PDB-7m6p: Full length alpha1 Glycine receptor in presence of 1mM Glycine Method: EM (single particle) / Resolution: 3.28 Å 23704 7m6q EMDB-23704, PDB-7m6q: Full length alpha1 Glycine receptor in presence of 1mM Glycine and 32uM Tetrahydrocannabinol State 1 Method: EM (single particle) / Resolution: 2.91 Å 23705 7m6r EMDB-23705, PDB-7m6r: Full length alpha1 Glycine receptor in presence of 1mM Glycine and 32uM Tetrahydrocannabinol State 2 Method: EM (single particle) / Resolution: 3.57 Å 23706 7m6s EMDB-23706, PDB-7m6s: Full length alpha1 Glycine receptor in presence of 1mM Glycine and 32uM Tetrahydrocannabinol State 3 Method: EM (single particle) / Resolution: 3.61 Å
Chemicals	ChemComp-TCI: (6aR,10aR)-6,6,9-trimethyl-3-pentyl-6a,7,8,10a-tetrahydro-6H-benzo[c]chromen-1-ol ChemComp-GLY: GLYCINE ChemComp-NAG: 2-acetamido-2-deoxy-beta-D-glucopyranose
Source	danio rerio (zebrafish)
Keywords	MEMBRANE PROTEIN / Ions Ligands Receptors / Glycine receptor Recombinant Proteins