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	Mechanisms of activation and desensitization of full-length glycine receptor in lipid nanodiscs.
Journal, issue, pages	Nat Commun, Vol. 11, Issue 1, Page 3752, Year 2020
Publish date	Jul 27, 2020
Authors	Arvind Kumar / Sandip Basak / Shanlin Rao / Yvonne Gicheru / Megan L Mayer / Mark S P Sansom / Sudha Chakrapani /
PubMed Abstract	Glycinergic synapses play a central role in motor control and pain processing in the central nervous system. Glycine receptors (GlyRs) are key players in mediating fast inhibitory neurotransmission ...Glycinergic synapses play a central role in motor control and pain processing in the central nervous system. Glycine receptors (GlyRs) are key players in mediating fast inhibitory neurotransmission at these synapses. While previous high-resolution structures have provided insights into the molecular architecture of GlyR, several mechanistic questions pertaining to channel function are still unanswered. Here, we present Cryo-EM structures of the full-length GlyR protein complex reconstituted into lipid nanodiscs that are captured in the unliganded (closed), glycine-bound (open and desensitized), and allosteric modulator-bound conformations. A comparison of these states reveals global conformational changes underlying GlyR channel gating and modulation. The functional state assignments were validated by molecular dynamics simulations, and the observed permeation events are in agreement with the anion selectivity and conductance of GlyR. These studies provide the structural basis for gating, ion selectivity, and single-channel conductance properties of GlyR in a lipid environment.
External links	Nat Commun / PubMed:32719334 / PubMed Central
Methods	EM (single particle)
Resolution	3.07 - 3.55 Å
Structure data	20714 6ubs EMDB-20714, PDB-6ubs: Full length Glycine receptor reconstituted in lipid nanodisc in Apo/Resting conformation Method: EM (single particle) / Resolution: 3.33 Å 20715 6ubt EMDB-20715, PDB-6ubt: Full length Glycine receptor reconstituted in lipid nanodisc in Gly-bound desensitized conformation Method: EM (single particle) / Resolution: 3.55 Å 20731 6ud3 EMDB-20731, PDB-6ud3: Full length Glycine receptor reconstituted in lipid nanodisc in Gly/PTX-bound open/blocked conformation Method: EM (single particle) / Resolution: 3.5 Å 21234 6vm0 EMDB-21234, PDB-6vm0: Full length Glycine receptor reconstituted in lipid nanodisc in Gly/IVM-conformation (State-1) Method: EM (single particle) / Resolution: 3.14 Å 21236 6vm2 EMDB-21236, PDB-6vm2: Full length Glycine receptor reconstituted in lipid nanodisc in Gly/IVM-conformation (State-2) Method: EM (single particle) / Resolution: 3.34 Å 21237 6vm3 EMDB-21237, PDB-6vm3: Full length Glycine receptor reconstituted in lipid nanodisc in Gly/IVM-conformation (State-3) Method: EM (single particle) / Resolution: 3.07 Å
Chemicals	ChemComp-PX4: 1,2-DIMYRISTOYL-SN-GLYCERO-3-PHOSPHOCHOLINE / DMPC, phospholipidYM / Dimyristoylphosphatidylcholine ChemComp-PIO: [(2R)-2-octanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phosphoryl]oxy-propyl] octanoate ChemComp-GLY: GLYCINE / Glycine ChemComp-NAG: 2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine ChemComp-RI5: (1aR,2aR,3S,6R,6aS,8aS,8bR,9R)-2a-hydroxy-8b-methyl-9-(prop-1-en-2-yl)hexahydro-3,6-methano-1,5,7-trioxacyclopenta[ij]c / toxinYM / Picrotoxin ChemComp-IVM: (2aE,4E,5'S,6S,6'R,7S,8E,11R,13R,15S,17aR,20R,20aR,20bS)-6'-[(2S)-butan-2-yl]-20,20b-dihydroxy-5',6,8,19-tetramethyl-17 / antiparasitic*YM / Ivermectin
Source	danio rerio (zebrafish)
Keywords	MEMBRANE PROTEIN / Ions Ligands Receptors / Glycine receptor Recombinant Proteins Glycine