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

@article{Bong2008StructuralSO,
  title={Structural studies of human brain-type creatine kinase complexed with the ADP-Mg2+-NO3- -creatine transition-state analogue complex.},
  author={Seoung Min Bong and Jin Ho Moon and Ki Hyun Nam and Ki Seog Lee and Young Min Chi and Kwang Yeon Hwang},
  journal={FEBS letters},
  year={2008},
  volume={582 28},
  pages={3959-65}
}
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… CONTINUE READING

From This Paper

Topics from this paper.
15 Citations
0 References
Similar Papers

Citations

Publications citing this paper.
Showing 1-10 of 15 extracted citations

Similar Papers

Loading similar papers…