3DRE

Crystal structure of Human Brain-type Creatine Kinase

3DRE の概要

• エントリーDOI: 10.2210/pdb3dre/pdb
• 関連するPDBエントリー: 3B6R 3DRB
• 分子名称: Creatine kinase B-type (2 entities in total)
• 機能のキーワード: human, creatine kinase, atp-binding, cytoplasm, kinase, nucleotide-binding, phosphoprotein, polymorphism, transferase
• 由来する生物種: Homo sapiens (Human)
• 細胞内の位置: Cytoplasm: P12277
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 85398.41

構造登録者

Moon, J.H.,Bong, S.M.,Hwang, K.Y.,Chi, Y.M. (登録日: 2008-07-11, 公開日: 2009-03-17, 最終更新日: 2024-03-20)

主引用文献

Bong, S.M.,Moon, J.H.,Nam, K.H.,Lee, K.S.,Chi, Y.M.,Hwang, K.Y.
Structural studies of human brain-type creatine kinase complexed with the ADP-Mg2+-NO3- -creatine transition-state analogue complex
Febs Lett., 582:3959-3965, 2008

PubMed 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 2.2A; 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.

PubMed: 18977227
DOI: 10.1016/j.febslet.2008.10.039

実験手法

X-RAY DIFFRACTION (2.2 Å)