Impact of intra-subunit domain-domain interactions on creatine kinase activity and stability

Tong Jin Zhao, Shan Feng, Yong Liang Wang, Yang Liu, Xue Chun Luo, Hai Meng Zhou, Yong Bin Yan

Research output: Contribution to journalArticle

27 Scopus citations

Abstract

Creatine kinase (CK) is a key enzyme in vertebrate excitable tissues. In this research, five conserved residues located on the intra-subunit domain-domain interface were mutated to explore their role in the activity and structural stability of CK. The mutations of Val72 and Gly73 decreased both the activity and stability of CK. The mutations of Cys74 and Val75, which had no significant effect on CK activity and structure, gradually decreased the stability and reactivation of CK. Our results suggested that the mutations might modify the correct positioning of the loop contributing to domain-domain interactions, and result in decreased stability against denaturation.

Original languageEnglish (US)
Pages (from-to)3835-3840
Number of pages6
JournalFEBS Letters
Volume580
Issue number16
DOIs
StatePublished - Jul 10 2006

Keywords

  • Creatine kinase
  • Domain-domain interactions
  • Folding intermediate
  • Phosphagen kinase
  • Structural stability

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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    Zhao, T. J., Feng, S., Wang, Y. L., Liu, Y., Luo, X. C., Zhou, H. M., & Yan, Y. B. (2006). Impact of intra-subunit domain-domain interactions on creatine kinase activity and stability. FEBS Letters, 580(16), 3835-3840. https://doi.org/10.1016/j.febslet.2006.05.076