Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6COY

Human CLC-1 chloride ion channel, transmembrane domain

Summary for 6COY
Entry DOI10.2210/pdb6coy/pdb
Related6COZ
EMDB information7544 7545
DescriptorChloride channel protein 1, CHLORIDE ION (2 entities in total)
Functional Keywordschloride, channel, clc, transport protein
Biological sourceHomo sapiens (Human)
Total number of polymer chains2
Total formula weight217608.16
Authors
Park, E.,MacKinnon, R. (deposition date: 2018-03-13, release date: 2018-06-13, Last modification date: 2024-03-13)
Primary citationPark, 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: 29809153
DOI: 10.7554/eLife.36629
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.36 Å)
Structure validation

227561

PDB entries from 2024-11-20

PDB statisticsPDBj update infoContact PDBjnumon