Secondary and tertiary structure of nucleotide-binding domain of alphasubunit of Na+/K+-ATPase

Biopolymers. 2002;67(4-5):242-6. doi: 10.1002/bip.10093.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphate / metabolism
  • Animals
  • Brain / enzymology
  • Circular Dichroism
  • Escherichia coli / metabolism
  • Mice
  • Models, Molecular
  • Protein Binding
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Sodium-Potassium-Exchanging ATPase / chemistry*
  • Sodium-Potassium-Exchanging ATPase / metabolism
  • Spectrum Analysis, Raman

Substances

  • Adenosine Triphosphate
  • Sodium-Potassium-Exchanging ATPase