Secondary and tertiary structure of nucleotide-binding domain of αsubunit of Na+/K+-ATPase-Reference-Cited by-同舟云学术

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

Published:2002 Issue:4-5 Volume:67 Page:242-246
ISSN:0006-3525
Container-title:Biopolymers
language:en
Short-container-title:Biopolymers

Author:

Hofbauerová Kateřina,Kopecký Vladimír,Ettrich Rüdiger,Ettrichová Olga,Amler Evžen

Funder

Ministry of Education of the Czech Republic

Volkswagen Foundation

GACR

Publisher

Wiley

Subject

Organic Chemistry,Biomaterials,Biochemistry,General Medicine,Biophysics

Reference20 articles.

1. Structure, function and regulation of Na,K-ATPase in the kidney

2. Binding of pyrene isothiocyanate to the E1ATP site makes the H4-H5 cytoplasmic loop of Na+/K+-ATPase rigid

3. The isolated H4-H5cytoplasmic loop of Na,K-ATPase overexpressed inEscherichia coliretains its ability to bind ATP

4. Three-dimensional structure of the large cytoplasmic H 4 ?H 5 loop of Na + /K + -ATPase deduced by restraint-based comparative modeling shows only one ATP binding site

Cited by 7 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. The phosphatase activity of the isolated H4-H5 loop of Na+/K+ ATPase resides outside its ATP binding site;European Journal of Biochemistry;2004-09-16

2. The Hydrogen Bonds between Arg423 and Glu472 and Other Key Residues, Asp443, Ser477, and Pro489, Are Responsible for the Formation and a Different Positioning of TNP-ATP and ATP within the Nucleotide-Binding Site of Na+/K+-ATPase;Biochemistry;2004-06-10

3. Vibrational spectroscopy and computer modeling of proteins: solving structure of α1-acid glycoprotein;Spectroscopy;2004

4. ATP-binding is stabilized by a stacking interaction within the binding site of Na+/K+-ATPase;Biochemical and Biophysical Research Communications;2003-06

5. Eight Amino Acids Form the ATP Recognition Site of Na+/K+-ATPase;Biochemistry;2003-05-09

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