Short transient receptor potential channel: Difference between revisions
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==Overview of the TRPC1/TRPC4 Channel== | ==Overview of the TRPC1/TRPC4 Channel== | ||
<StructureSection load='8WPL' size='340' side='right' caption='Cryo-EM structure of the heteromeric human TRPC1/TRPC4 channel (PDB: | <StructureSection load='8WPL' size='340' side='right' caption='Cryo-EM structure of the heteromeric human TRPC1/TRPC4 channel (PDB: 8wpl)' scene=''> | ||
This paper shows the detailed 3D structure of the human TRPC1-TRPC4 ion channel. This channel is made of one TRPC1 nd three TRPC4 subunits. The researchers captured(using cro-Electron Microscopy) what the channel looks like normally and when blocked by a drug, Pico145. <ref>Won, J., Kim, J., Kim, J. et al. (2025). Cryo-EM structure of the heteromeric TRPC1/TRPC4 channel. ''Nature Structural & Molecular Biology'', 32(2):326–338. DOI: 10.1038/s41594-024-01408-1</ref> | This paper shows the detailed 3D structure of the human TRPC1-TRPC4 ion channel. This channel is made of one TRPC1 nd three TRPC4 subunits. The researchers captured(using cro-Electron Microscopy) what the channel looks like normally and when blocked by a drug, Pico145. <ref>Won, J., Kim, J., Kim, J. et al. (2025). Cryo-EM structure of the heteromeric TRPC1/TRPC4 channel. ''Nature Structural & Molecular Biology'', 32(2):326–338. DOI: 10.1038/s41594-024-01408-1</ref> | ||
Main finding: The incorporation of one TRPC1 completely changes the shape of the TRPC4 channel. It changes TRPC4 from a perfectly symmetrical pore to an asymmetric heteromer(TRPC1/TRPC4). This asymmetry narrows the ion pathway, bends several helices, and creates a different lower gate. This decreases the calcium permeability and shifts the preference to monovalent ions such as sodium and potassium. Electrical tests and mutant experiments confirm that this structural shift affects how the channel actually works.<ref>Won, J., Kim, J., Kim, J. et al. (2025). Cryo-EM structure of the heteromeric TRPC1/TRPC4 channel. ''Nature Structural & Molecular Biology'', 32(2):326–338. DOI: 10.1038/s41594-024-01408-1</ref> | Main finding: The incorporation of one TRPC1 completely changes the shape of the TRPC4 channel. It changes TRPC4 from a perfectly symmetrical pore to an asymmetric heteromer(TRPC1/TRPC4). This asymmetry narrows the ion pathway, bends several helices, and creates a different lower gate. This decreases the calcium permeability and shifts the preference to monovalent ions such as sodium and potassium. Electrical tests and mutant experiments confirm that this structural shift affects how the channel actually works.<ref>Won, J., Kim, J., Kim, J. et al. (2025). Cryo-EM structure of the heteromeric TRPC1/TRPC4 channel. ''Nature Structural & Molecular Biology'', 32(2):326–338. DOI: 10.1038/s41594-024-01408-1</ref> | ||
