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PeerJ. 2017 Mar 14;5:e3087. doi: 10.7717/peerj.3087. eCollection 2017.

Computer modelling reveals new conformers of the ATP binding loop of Na.

PeerJ

Gracian Tejral, Bruno Sopko, Alois Necas, Wilhelm Schoner, Evzen Amler

Affiliations

  1. Department of Biophysics, 2nd Faculty of Medicine, Charles University Prague, Prague, Czech Republic; Laboratory of Tissue Engineering, Institute of Experimental Medicine, Academy of Sciences of the Czech Republic, Prague, Czech Republic.
  2. Department of Medical Chemistry and Clinical Biochemistry, 2nd Faculty of Medicine, Charles University Prague , Prague , Czech Republic.
  3. Small Animal Clinic, Faculty of Veterinary Medicine, University of Veterinary and Pharmaceutical Science , Brno , Czech Republic.
  4. Institute of Biochemistry and Endocrinology, University of Giessen , Giessen , Germany.

PMID: 28316890 PMCID: PMC5354106 DOI: 10.7717/peerj.3087

Abstract

Hydrolysis of ATP by Na

Keywords: Hinge movement; M4M5 loop; Na+/K+-ATPase phosphorylation; Open and closed conformations

Conflict of interest statement

The authors declare there are no competing interests.

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