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Structural studies of human brain-type creatine kinase complexed with the ADP–Mg2+–NO3−–creatine transition-state analogue complex
- Source :
-
FEBS Letters . Nov2008, Vol. 582 Issue 28, p3959-3965. 7p. - Publication Year :
- 2008
-
Abstract
- Abstract: 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 2.2Å; the ADP–Mg2+, nitrate, and creatine complex (transition-state-analogue complex; TSAC); and the ADP–Mg2+-complex at 2.0Å. 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. [Copyright &y& Elsevier]
Details
- Language :
- English
- ISSN :
- 00145793
- Volume :
- 582
- Issue :
- 28
- Database :
- Academic Search Index
- Journal :
- FEBS Letters
- Publication Type :
- Academic Journal
- Accession number :
- 35328880
- Full Text :
- https://doi.org/10.1016/j.febslet.2008.10.039