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PDB: 9 results
9B90
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BU of 9b90 by Molmil
Cryo-EM structure of the human TRPM4 channel in complex with calcium and ATP at 37 degrees Celsius
Descriptor: ADENOSINE-5'-TRIPHOSPHATE, CALCIUM ION, Transient receptor potential cation channel subfamily M member 4
Authors:Hu, J, Lu, W, Du, J.
Deposit date:2024-04-01
Release date:2024-05-15
Last modified:2024-06-26
Method:ELECTRON MICROSCOPY (3.4 Å)
Cite:Physiological temperature drives TRPM4 ligand recognition and gating.
Nature, 630, 2024
9B8Z
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BU of 9b8z by Molmil
Cryo-EM structure of the human TRPM4 channel subunit in complex with calcium and decavanadate at 37 degrees Celsius
Descriptor: CALCIUM ION, DECAVANADATE, Transient receptor potential cation channel subfamily M member 4
Authors:Hu, J, Lu, W, Du, J.
Deposit date:2024-04-01
Release date:2024-05-15
Last modified:2024-06-26
Method:ELECTRON MICROSCOPY (3.4 Å)
Cite:Physiological temperature drives TRPM4 ligand recognition and gating.
Nature, 630, 2024
9B8X
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BU of 9b8x by Molmil
Cryo-EM structure of the human TRPM4 channel subunit in complex with calcium 37 degrees Celsius
Descriptor: CALCIUM ION, Transient receptor potential cation channel subfamily M member 4
Authors:Hu, J, Lu, W, Du, J.
Deposit date:2024-04-01
Release date:2024-05-15
Last modified:2024-06-26
Method:ELECTRON MICROSCOPY (3 Å)
Cite:Physiological temperature drives TRPM4 ligand recognition and gating.
Nature, 630, 2024
9B8Y
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BU of 9b8y by Molmil
Cryo-EM structure of the human TRPM4 channel in complex with calcium and decavanadate at 37 degrees Celsius
Descriptor: CALCIUM ION, DECAVANADATE, Transient receptor potential cation channel subfamily M member 4
Authors:Hu, J, Lu, W, Du, J.
Deposit date:2024-04-01
Release date:2024-05-15
Last modified:2024-06-26
Method:ELECTRON MICROSCOPY (3.2 Å)
Cite:Physiological temperature drives TRPM4 ligand recognition and gating.
Nature, 630, 2024
9B93
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BU of 9b93 by Molmil
Cryo-EM structure of the human TRPM4 channel in the presence of EDTA at 37 degrees Celsius
Descriptor: Transient receptor potential cation channel subfamily M member 4
Authors:Hu, J, Lu, W, Du, J.
Deposit date:2024-04-01
Release date:2024-05-15
Last modified:2024-06-26
Method:ELECTRON MICROSCOPY (3.1 Å)
Cite:Physiological temperature drives TRPM4 ligand recognition and gating.
Nature, 630, 2024
9B92
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BU of 9b92 by Molmil
Cryo-EM structure of the human TRPM4 in complex with calcium at 18 degrees Celsius
Descriptor: CALCIUM ION, Transient receptor potential cation channel subfamily M member 4
Authors:Hu, J, Lu, W, Du, J.
Deposit date:2024-04-01
Release date:2024-05-15
Last modified:2024-06-26
Method:ELECTRON MICROSCOPY (3.5 Å)
Cite:Physiological temperature drives TRPM4 ligand recognition and gating.
Nature, 630, 2024
9B91
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BU of 9b91 by Molmil
Cryo-EM structure of the human TRPM4 channel subunit in complex with calcium and ATP at 37 degrees Celsius
Descriptor: ADENOSINE-5'-TRIPHOSPHATE, CALCIUM ION, Transient receptor potential cation channel subfamily M member 4
Authors:Hu, J, Lu, W, Du, J.
Deposit date:2024-04-01
Release date:2024-05-15
Last modified:2024-06-26
Method:ELECTRON MICROSCOPY (3.3 Å)
Cite:Physiological temperature drives TRPM4 ligand recognition and gating.
Nature, 630, 2024
9B8W
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BU of 9b8w by Molmil
Cryo-EM structure of the human TRPM4 in complex with calcium at 37 degrees Celsius
Descriptor: CALCIUM ION, Transient receptor potential cation channel subfamily M member 4
Authors:Hu, J, Lu, W, Du, J.
Deposit date:2024-04-01
Release date:2024-05-15
Last modified:2024-06-26
Method:ELECTRON MICROSCOPY (3.1 Å)
Cite:Physiological temperature drives TRPM4 ligand recognition and gating.
Nature, 630, 2024
9B94
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BU of 9b94 by Molmil
Cryo-EM structure of the E396A mutant of human TRPM4 in complex with calcium at 37 degrees Celsius
Descriptor: CALCIUM ION, Transient receptor potential cation channel subfamily M member 4
Authors:Hu, J, Lu, W, Du, J.
Deposit date:2024-04-01
Release date:2024-05-22
Last modified:2024-06-26
Method:ELECTRON MICROSCOPY (3.1 Å)
Cite:Physiological temperature drives TRPM4 ligand recognition and gating.
Nature, 630, 2024

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PDB entries from 2024-07-03

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