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PDBsum entry 3b6r
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References listed in PDB file
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Key reference
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Title
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Structural studies of human brain-Type creatine kinase complexed with the ADP-Mg2+-No3- -Creatine transition-State analogue complex.
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Authors
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S.M.Bong,
J.H.Moon,
K.H.Nam,
K.S.Lee,
Y.M.Chi,
K.Y.Hwang.
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Ref.
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Febs Lett, 2008,
582,
3959-3965.
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PubMed id
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Abstract
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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.
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