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

FEBS Lett. 2008 Nov 26;582(28):3959-65. doi: 10.1016/j.febslet.2008.10.039. Epub 2008 Oct 31.


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 2.2A; the ADP-Mg2+, nitrate, and creatine complex (transition-state-analogue complex; TSAC); and the ADP-Mg2+-complex at 2.0A. 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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Diphosphate / chemistry*
  • Creatine Kinase, BB Form / chemistry*
  • Crystallography, X-Ray
  • Humans
  • Magnesium / chemistry*
  • Nitrogen Oxides / chemistry*
  • Protein Conformation
  • Protein Folding


  • Nitrogen Oxides
  • nitrogen trioxide
  • Adenosine Diphosphate
  • Creatine Kinase, BB Form
  • Magnesium