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- W2026773721 abstract "The cardiac Na (+)-Ca (2+) exchanger (NCX1) is modeled to contain nine transmembrane segments (TMS) with a pair of oppositely oriented, conserved sequences called the alpha-repeats that are important in ion transport. Residue 122 in the alpha-1 repeat is in proximity to residue 768 in TMS 6, and the two residues can be cross-linked . During studies on the substrate specificity of this intramolecular cross-link, we found evidence that NCX1 can form dimers. At 37 degrees C in the absence of extracellular Na (+), copper phenanthroline catalyzes disulfide bond formation between cysteines at position 122 in adjacent NCX1 proteins. Dimerization was confirmed by histidine tag pull-down experiments that demonstrate the association of untagged NCX1 with histidine-tagged NCX1. Dimerization occurs along a face of the protein that includes parts of the alpha-1 and alpha-2 repeats as well as parts of TMS 1 and TMS 2. We do not see cross-linking between residues in TMS 5, TMS 6, or TMS 7. These data provide the first evidence for dimer formation by the Na (+)-Ca (2+) exchanger." @default.
- W2026773721 created "2016-06-24" @default.
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- W2026773721 date "2008-05-09" @default.
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- W2026773721 title "Intermolecular Cross-Linking of Na<sup>+</sup>−Ca<sup>2+</sup> Exchanger Proteins: Evidence for Dimer Formation" @default.
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- W2026773721 doi "https://doi.org/10.1021/bi800177t" @default.
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