7ZK3
 
 | | Structure of 1PBC- and calcium-bound mTMEM16A(ac) chloride channel at 2.85 A resolution | | Descriptor: | 1-Hydroxy-3-(trifluoromethyl)pyrido[1,2-a]benzimidazole-4-carbonitrile, Anoctamin-1, CALCIUM ION | | Authors: | Lam, A.K.M, Rutz, S, Dutzler, R. | | Deposit date: | 2022-04-12 | | Release date: | 2022-05-25 | | Last modified: | 2022-06-01 | | Method: | ELECTRON MICROSCOPY (2.85 Å) | | Cite: | Inhibition mechanism of the chloride channel TMEM16A by the pore blocker 1PBC.
Nat Commun, 13, 2022
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7B5D
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7B5E
 | | Structure of calcium-bound mTMEM16A(ac)-I551A chloride channel at 4.1 A resolution | | Descriptor: | Anoctamin-1, CALCIUM ION | | Authors: | Lam, A.K.M, Rheinberger, J, Paulino, C, Dutzler, R. | | Deposit date: | 2020-12-03 | | Release date: | 2021-02-10 | | Last modified: | 2021-02-17 | | Method: | ELECTRON MICROSCOPY (4.1 Å) | | Cite: | Gating the pore of the calcium-activated chloride channel TMEM16A.
Nat Commun, 12, 2021
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7B5C
 | | Structure of calcium-bound mTMEM16A(ac) chloride channel at 3.7 A resolution | | Descriptor: | Anoctamin-1, CALCIUM ION | | Authors: | Lam, A.K.M, Rheinberger, J, Paulino, C, Dutzler, R. | | Deposit date: | 2020-12-03 | | Release date: | 2021-02-10 | | Last modified: | 2021-02-17 | | Method: | ELECTRON MICROSCOPY (3.7 Å) | | Cite: | Gating the pore of the calcium-activated chloride channel TMEM16A.
Nat Commun, 12, 2021
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6FNW
 | | Structure of a volume-regulated anion channel of the LRRC8 family | | Descriptor: | 1,2-ETHANEDIOL, Volume-regulated anion channel subunit LRRC8A | | Authors: | Deneka, D, Sawicka, M, Lam, A.K.M, Paulino, C, Dutzler, R. | | Deposit date: | 2018-02-05 | | Release date: | 2018-05-16 | | Last modified: | 2018-06-27 | | Method: | X-RAY DIFFRACTION (1.8 Å) | | Cite: | Structure of a volume-regulated anion channel of the LRRC8 family.
Nature, 558, 2018
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6G9O
 | | Structure of full-length homomeric mLRRC8A volume-regulated anion channel at 4.25 A resolution | | Descriptor: | Volume-regulated anion channel subunit LRRC8A | | Authors: | Sawicka, M, Deneka, D, Lam, A.K.M, Paulino, C, Dutzler, R. | | Deposit date: | 2018-04-11 | | Release date: | 2018-05-16 | | Last modified: | 2019-12-11 | | Method: | ELECTRON MICROSCOPY (4.25 Å) | | Cite: | Structure of a volume-regulated anion channel of the LRRC8 family.
Nature, 558, 2018
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6G8Z
 | | Structure of the pore domain of homomeric mLRRC8A volume-regulated anion channel at 3.66 A resolution | | Descriptor: | Volume-regulated anion channel subunit LRRC8A | | Authors: | Sawicka, M, Deneka, D, Lam, A.K.M, Paulino, C, Dutzler, R. | | Deposit date: | 2018-04-10 | | Release date: | 2018-05-16 | | Last modified: | 2019-12-11 | | Method: | ELECTRON MICROSCOPY (3.66 Å) | | Cite: | Structure of a volume-regulated anion channel of the LRRC8 family.
Nature, 558, 2018
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6G9L
 | | Structure of homomeric mLRRC8A volume-regulated anion channel at 5.01 A resolution | | Descriptor: | Volume-regulated anion channel subunit LRRC8A | | Authors: | Sawicka, M, Deneka, D, Lam, A.K.M, Paulino, C, Dutzler, R. | | Deposit date: | 2018-04-11 | | Release date: | 2018-05-16 | | Last modified: | 2019-12-11 | | Method: | ELECTRON MICROSCOPY (5.01 Å) | | Cite: | Structure of a volume-regulated anion channel of the LRRC8 family.
Nature, 558, 2018
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8QZC
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5OYB
 | | Structure of calcium-bound mTMEM16A chloride channel at 3.75 A resolution | | Descriptor: | Anoctamin-1, CALCIUM ION | | Authors: | Paulino, C, Kalienkova, V, Lam, K.M, Neldner, Y, Dutzler, R. | | Deposit date: | 2017-09-08 | | Release date: | 2017-12-20 | | Last modified: | 2019-12-11 | | Method: | ELECTRON MICROSCOPY (3.75 Å) | | Cite: | Activation mechanism of the calcium-activated chloride channel TMEM16A revealed by cryo-EM.
Nature, 552, 2017
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5OYG
 | | Structure of calcium-free mTMEM16A chloride channel at 4.06 A resolution | | Descriptor: | Anoctamin-1 | | Authors: | Paulino, C, Kalienkova, V, Lam, K.M, Neldner, Y, Dutzler, R. | | Deposit date: | 2017-09-08 | | Release date: | 2017-12-20 | | Last modified: | 2019-12-11 | | Method: | ELECTRON MICROSCOPY (4.06 Å) | | Cite: | Activation mechanism of the calcium-activated chloride channel TMEM16A revealed by cryo-EM.
Nature, 552, 2017
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