2ja3 | pdb_00002ja3

CYTOPLASMIC DOMAIN OF THE HUMAN CHLORIDE TRANSPORTER CLC-5 IN COMPLEX WITH ADP

spinqualitylabelsall models 2ja3, resolution 3.05Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2ja3 is a 6 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ADP Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The ubiquitous CBS domains, which are found as part of cytoplasmic domains in the ClC family of chloride channels and transporters, have previously been identified as building blocks for regulatory nucleotide-binding sites. Here we report the structures of the cytoplasmic domain of the human transporter ClC-5 in complex with ATP and ADP. The nucleotides bind to a specific site in the protein. As determined by equilibrium dialysis, the affinities for ATP, ADP and AMP are in the high micromolar range. Point mutations that interfere with nucleotide binding change the transport behavior of a ClC-5 mutant expressed in Xenopus laevis oocytes. Our results establish the structural and energetic basis for the interaction of ClC-5 with nucleotides and provide a framework for future investigations. Nucleotide recognition by the cytoplasmic domain of the human chloride transporter ClC-5.,Meyer S, Savaresi S, Forster IC, Dutzler R Nat Struct Mol Biol. 2007 Jan;14(1):60-7. Epub 2006 Dec 31. PMID:17195847 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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