6COZ
Human CLC-1 chloride ion channel, C-terminal cytosolic domain
Summary for 6COZ
| Entry DOI | 10.2210/pdb6coz/pdb |
| Related | 6COY |
| EMDB information | 7544 7545 |
| Descriptor | Chloride channel protein 1 (1 entity in total) |
| Functional Keywords | chloride, channel, clc, transport protein |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 2 |
| Total formula weight | 217466.34 |
| Authors | Park, E.,MacKinnon, R. (deposition date: 2018-03-13, release date: 2018-06-13, Last modification date: 2024-03-13) |
| Primary citation | Park, E.,MacKinnon, R. Structure of the CLC-1 chloride channel fromHomo sapiens. Elife, 7:-, 2018 Cited by PubMed Abstract: CLC channels mediate passive Cl conduction, while CLC transporters mediate active Cl transport coupled to H transport in the opposite direction. The distinction between CLC-0/1/2 channels and CLC transporters seems undetectable by amino acid sequence. To understand why they are different functionally we determined the structure of the human CLC-1 channel. Its 'glutamate gate' residue, known to mediate proton transfer in CLC transporters, adopts a location in the structure that appears to preclude it from its transport function. Furthermore, smaller side chains produce a wider pore near the intracellular surface, potentially reducing a kinetic barrier for Cl conduction. When the corresponding residues are mutated in a transporter, it is converted to a channel. Finally, Cl at key sites in the pore appear to interact with reduced affinity compared to transporters. Thus, subtle differences in glutamate gate conformation, internal pore diameter and Cl affinity distinguish CLC channels and transporters. PubMed: 29809153DOI: 10.7554/eLife.36629 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.36 Å) |
Structure validation
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