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filingDate 1998-07-17-04:00^^<http://www.w3.org/2001/XMLSchema#date>
publicationDate 2001-07-31-04:00^^<http://www.w3.org/2001/XMLSchema#date>
publicationNumber JP-2001510166-A
titleOfInvention Structure of ankyrin-binding domain of α-Na, K-ATPase
abstract (57) [Summary]nThe association between ankyrin and the universal membrane proteins α-Na, K-ATPase, which are critical for the vector-wise transport of ions and nutrients, allows the assembly and stabilization of Na, K-ATPase in the membrane. is necessary. The present invention relates to the discovery that α-Na, K-ATPase is located in its second putative cytoplasmic domain, mainly through residues 142-166 (minimal ankyrin binding domain), in red blood cells (ANK1) and Madin Darby canine kidney. (MDCK) is directed to the disclosure of binding to both cellular ankyrin (ANK3). A glutathione-S-transferase fusion peptide incorporating these residues binds specifically to ankyrin. The three-dimensional structure of the minimal binding domain of the fusion peptide (2.6 °) reveals, for the first time, a seven-residue loop with two charged hydrophilic faces that caps the double β-strand. The invention includes peptides containing the minimal binding domain and analogs of these peptides. Another aspect of the invention includes a method for elucidating the minimal ankyrin binding domain (s) of other proteins that interact with ankyrin. Finally, the present invention relates to a method of screening for a compound that inhibits or enhances the binding of α-Na, K-ATPase or other ankyrin-binding protein to ankyrin, and ankyrin, and a protein that binds to the compound together with the compound. And a method for modulating the interaction between
priorityDate 1997-07-18-04:00^^<http://www.w3.org/2001/XMLSchema#date>
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