2PFI

Crystal structure of the cytoplasmic domain of the human chloride channel ClC-Ka

Summary for 2PFI

• Entry DOI: 10.2210/pdb2pfi/pdb
• Descriptor: Chloride channel protein ClC-Ka, IODIDE ION, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: cystathionine beta synthetase (cbs) domains containing protein, transport protein
• Biological source: Homo sapiens (human)
• Cellular location: Membrane; Multi-pass membrane protein: P51800
• Total number of polymer chains: 2
• Total formula weight: 36532.89

Authors

Markovic, S.,Dutzler, R. (deposition date: 2007-04-05, release date: 2007-06-19, Last modification date: 2024-02-21)

Primary citation

Markovic, S.,Dutzler, R.
The Structure of the Cytoplasmic Domain of the Chloride Channel ClC-Ka Reveals a Conserved Interaction Interface.
Structure, 15:715-725, 2007

PubMed Abstract: The cytoplasmic domains of ClC chloride channels and transporters are ubiquitously found in eukaryotic family members and have been suggested to be involved in the regulation of ion transport. All cytoplasmic ClC domains share a conserved scaffold that contains a pair of CBS motifs. Here we describe the structure of the cytoplasmic component of the human chloride channel ClC-Ka at 1.6 A resolution. The structure reveals a dimeric organization of the domain that is unusual for CBS motif containing proteins. Using a biochemical approach combining mutagenesis, crosslinking, and analytical ultracentrifugation, we demonstrate that the interaction interface is preserved in solution and that the distantly related channel ClC-0 likely exhibits a similar structural organization. Our results reveal a conserved interaction interface that relates the cytoplasmic domains of ClC proteins and establish a structural relationship that is likely general for this important family of transport proteins.

PubMed: 17562318
DOI: 10.1016/j.str.2007.04.013

Experimental method

X-RAY DIFFRACTION (1.6 Å)