2D4Z
Crystal structure of the cytoplasmic domain of the chloride channel ClC-0
Summary for 2D4Z
| Entry DOI | 10.2210/pdb2d4z/pdb |
| Descriptor | Chloride channel protein (1 entity in total) |
| Functional Keywords | clc chloride channel cytoplasmic domain, cbs domains, ion channel regulatory subunit, transport protein |
| Biological source | Torpedo marmorata (marbled electric ray) |
| Cellular location | Membrane; Multi-pass membrane protein: P21564 |
| Total number of polymer chains | 2 |
| Total formula weight | 55573.67 |
| Authors | Dutzler, R.,Meyer, S. (deposition date: 2005-10-26, release date: 2006-02-14, Last modification date: 2024-03-13) |
| Primary citation | Meyer, S.,Dutzler, R. Crystal structure of the cytoplasmic domain of the chloride channel ClC-0. Structure, 14:299-307, 2006 Cited by PubMed Abstract: Ion channels are frequently organized in a modular fashion and consist of a membrane-embedded pore domain and a soluble regulatory domain. A similar organization is found for the ClC family of Cl- channels and transporters. Here, we describe the crystal structure of the cytoplasmic domain of ClC-0, the voltage-dependent Cl- channel from T. marmorata. The structure contains a folded core of two tightly interacting cystathionine beta-synthetase (CBS) subdomains. The two subdomains are connected by a 96 residue mobile linker that is disordered in the crystals. As revealed by analytical ultracentrifugation, the domains form dimers, thereby most likely extending the 2-fold symmetry of the transmembrane pore. The structure provides insight into the organization of the cytoplasmic domains within the ClC family and establishes a framework for guiding future investigations on regulatory mechanisms. PubMed: 16472749DOI: 10.1016/j.str.2005.10.008 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.1 Å) |
Structure validation
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