Structural studies of human brain-type creatine kinase complexed with the ADP-Mg2+-NO3--creatine transition-state analogue complex

Seoung Min Bong, Jin Ho Moon, Ki Hyun Nam, Ki Seog Lee, Young Min Chi, Kwang Yeon Hwang

Research output: Contribution to journalArticlepeer-review

54 Citations (Scopus)


Creatine kinase is a member of the phosphagen kinase family, which catalyzes the reversible phosphoryl transfer reaction that occurs between ATP and creatine to produce ADP and phosphocreatine. Here, three structural aspects of human-brain-type-creatine-kinase (hBB-CK) were identified by X-ray crystallography: the ligand-free-form at 2.2 Å; the ADP-Mg2+, nitrate, and creatine complex (transition-state-analogue complex; TSAC); and the ADP-Mg2+-complex at 2.0 Å. The structures of ligand-bound hBB-CK revealed two different monomeric states in a single homodimer. One monomer is a closed form, either bound to TSAC or the ADP-Mg2+-complex, and the second monomer is an unliganded open form. These structural studies provide a detailed mechanism indicating that the binding of ADP-Mg2+ alone may trigger conformational changes in hBB-CK that were not observed with muscle-type-CK.

Original languageEnglish
Pages (from-to)3959-3965
Number of pages7
JournalFEBS Letters
Issue number28
Publication statusPublished - 2008 Nov 26


  • Brain-type creatine kinase
  • Creatine complex
  • Crystal structure
  • Energy homeostasis
  • Shuttle system

ASJC Scopus subject areas

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


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