6V0B
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![BU of 6v0b by Molmil](/molmil-images/mine/6v0b) | Unliganded ELIC in POPC-only nanodiscs. | Descriptor: | Gamma-aminobutyric-acid receptor subunit beta-1 | Authors: | Grosman, C, Kumar, P. | Deposit date: | 2019-11-18 | Release date: | 2020-01-15 | Last modified: | 2024-03-06 | Method: | ELECTRON MICROSCOPY (4.1 Å) | Cite: | Cryo-EM structures of a lipid-sensitive pentameric ligand-gated ion channel embedded in a phosphatidylcholine-only bilayer. Proc.Natl.Acad.Sci.USA, 117, 2020
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6V03
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![BU of 6v03 by Molmil](/molmil-images/mine/6v03) | ELIC-propylammonium complex in POPC-only nanodiscs | Descriptor: | 3-AMINOPROPANE, Gamma-aminobutyric-acid receptor subunit beta-1 | Authors: | Grosman, C, Kumar, P. | Deposit date: | 2019-11-18 | Release date: | 2020-01-15 | Last modified: | 2024-03-06 | Method: | ELECTRON MICROSCOPY (3.3 Å) | Cite: | Cryo-EM structures of a lipid-sensitive pentameric ligand-gated ion channel embedded in a phosphatidylcholine-only bilayer. Proc.Natl.Acad.Sci.USA, 117, 2020
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4LMK
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4LMJ
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4LML
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![BU of 4lml by Molmil](/molmil-images/mine/4lml) | GLIC double mutant I9'A T25'A | Descriptor: | Proton-gated ion channel | Authors: | Grosman, C, Gonzalez-Gutierrez, G. | Deposit date: | 2013-07-10 | Release date: | 2013-10-30 | Last modified: | 2023-09-20 | Method: | X-RAY DIFFRACTION (3.8 Å) | Cite: | Gating of the proton-gated ion channel from Gloeobacter violaceus at pH 4 as revealed by X-ray crystallography. Proc.Natl.Acad.Sci.USA, 110, 2013
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7L6Q
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![BU of 7l6q by Molmil](/molmil-images/mine/7l6q) | Unliganded ELIC in styrene-maleic-acid nanodiscs at 2.5-Angstrom resolution | Descriptor: | (1R)-2-{[(S)-{[(2S)-2,3-dihydroxypropyl]oxy}(hydroxy)phosphoryl]oxy}-1-[(hexadecanoyloxy)methyl]ethyl (9Z)-octadec-9-enoate, CARDIOLIPIN, Gamma-aminobutyric-acid receptor subunit beta-1 | Authors: | Grosman, C, Kumar, P. | Deposit date: | 2020-12-23 | Release date: | 2021-06-23 | Last modified: | 2024-03-06 | Method: | ELECTRON MICROSCOPY (2.5 Å) | Cite: | Structure and function at the lipid-protein interface of a pentameric ligand-gated ion channel. Proc.Natl.Acad.Sci.USA, 118, 2021
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5V6O
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5V6N
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7L6U
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3UQ4
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![BU of 3uq4 by Molmil](/molmil-images/mine/3uq4) | X-ray structure of a pentameric ligand gated ion channel from Erwinia chrysanthemi (ELIC) mutant F247L (F16L) | Descriptor: | Gamma-aminobutyric-acid receptor subunit beta-1, SODIUM ION | Authors: | Gonzalez-Gutierrez, G, Lukk, T, Agarwal, V, Papke, D, Nair, S.K, Grosman, C. | Deposit date: | 2011-11-19 | Release date: | 2012-04-04 | Last modified: | 2023-09-13 | Method: | X-RAY DIFFRACTION (3.5 Å) | Cite: | Mutations that stabilize the open state of the Erwinia chrisanthemi ligand-gated ion channel fail to change the conformation of the pore domain in crystals. Proc.Natl.Acad.Sci.USA, 109, 2012
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3UQ7
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![BU of 3uq7 by Molmil](/molmil-images/mine/3uq7) | X-ray structure of a pentameric ligand gated ion channel from Erwinia chrysanthemi (ELIC) mutant L240S F247L (L9S F16L) in presence of 10 mM cysteamine | Descriptor: | Gamma-aminobutyric-acid receptor subunit beta-1 | Authors: | Gonzalez-Gutierrez, G, Lukk, T, Agarwal, V, Papke, D, Nair, S.K, Grosman, C. | Deposit date: | 2011-11-19 | Release date: | 2012-04-04 | Last modified: | 2023-09-13 | Method: | X-RAY DIFFRACTION (3.8 Å) | Cite: | Mutations that stabilize the open state of the Erwinia chrisanthemi ligand-gated ion channel fail to change the conformation of the pore domain in crystals. Proc.Natl.Acad.Sci.USA, 109, 2012
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3UQ5
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![BU of 3uq5 by Molmil](/molmil-images/mine/3uq5) | X-ray structure of a pentameric ligand gated ion channel from Erwinia chrysanthemi (ELIC) mutant L240A F247L (L9A F16L) in the presence of 10 mM cysteamine | Descriptor: | Gamma-aminobutyric-acid receptor subunit beta-1, SODIUM ION | Authors: | Gonzalez-Gutierrez, G, Lukk, T, Agarwal, V, Papke, D, Nair, S.K, Grosman, C. | Deposit date: | 2011-11-19 | Release date: | 2012-04-04 | Last modified: | 2023-09-13 | Method: | X-RAY DIFFRACTION (4.2 Å) | Cite: | Mutations that stabilize the open state of the Erwinia chrisanthemi ligand-gated ion channel fail to change the conformation of the pore domain in crystals. Proc.Natl.Acad.Sci.USA, 109, 2012
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