Structural studies of human brain-type creatine kinase complexed with the ADP-Mg2+-NO3--creatine transition-state analogue complex
- Authors
- Bong, Seoung Min; Moon, Jin Ho; Nam, Ki Hyun; Lee, Ki Seog; Chi, Young Min; Hwang, Kwang Yeon
- Issue Date
- 26-11월-2008
- Publisher
- WILEY
- Keywords
- Brain-type creatine kinase; Shuttle system; Energy homeostasis; Crystal structure; Creatine complex
- Citation
- FEBS LETTERS, v.582, no.28, pp.3959 - 3965
- Indexed
- SCIE
SCOPUS
- Journal Title
- FEBS LETTERS
- Volume
- 582
- Number
- 28
- Start Page
- 3959
- End Page
- 3965
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/122383
- DOI
- 10.1016/j.febslet.2008.10.039
- ISSN
- 0014-5793
- 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 2.2 angstrom; the ADP-Mg2+, nitrate, and creatine complex (transition-state-analogue complex; TSAC); and the ADP-Mg2+-complex at 2.0 angstrom. 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. (C) 2008 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
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Collections - Graduate School > Department of Biosystems and Biotechnology > 1. Journal Articles
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