title: Secondary and tertiary structure of nucleotide-binding domain of alphasubunit of Na+/K+-ATPase.
abstract: The nucleotide-binding domain of the alpha subunit of mouse brain Na+/K+-ATPase was expressed and isolated from Escherichia coli cells. A model structure was constructed by comparative modeling with and without docked ATP. This was compared with the secondary structure determination from UV circular dichroism and Raman spectroscopy. Thus, we support the quality of the model and the correct folding of the recombinant protein. ATP binding was followed by Raman difference spectroscopy, and its influence on the secondary structure of the N domain seems to not be significant.
authors.affiliation: Department of Physical and Macromolecular Chemistry, Charles University, Albertov 2030, CZ-128 40 Prague 2, Czech Republic. hofbauer@biomed.cas.cz
authors.forename: Katerina
authors.initials: K
authors.lastname: Hofbauerová
authors.forename: Vladimír
authors.initials: V
authors.lastname: Kopecký
authors.forename: Rüdiger
authors.initials: R
authors.lastname: Ettrich
authors.forename: Olga
authors.initials: O
authors.lastname: Ettrichová
authors.forename: Evzen
authors.initials: E
authors.lastname: Amler
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D001921:Brain / Q000201:enzymology; D002942:Circular Dichroism; D004926:Escherichia coli / Q000378:metabolism; D051379:Mice; D008958:Models, Molecular; D011485:Protein Binding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D000254:Sodium-Potassium-Exchanging ATPase / Q000737:chemistry* / Q000378:metabolism; D013059:Spectrum Analysis, Raman
chemical_list: D000255:Adenosine Triphosphate; D000254:Sodium-Potassium-Exchanging ATPase