FEBS Letters · 1996 · 19 citations · 24 references
Life SciencesBiochemistryMolecular BiologyMolecular BiophysicsProtein BiochemistryStructural BiologyCalcium-binding ProteinsLigand BindingProtein ConformationProtein DomainsProtein StructureProtein-ligand BindingCalcium-binding Site StructureConformational Change DetectionFluorescence QuenchingIntrinsic FluorescenceMagnesium Interactions With CalciumMetal Ion CoordinationMetal Ion Coordination SitesMetal-binding Proteins
We demonstrated recently that coagulation factor IX has a specific binding site(s) for Mg2+ ions, independent of the (Ca2+)-binding sites, and that binding of Mg2+ ions is very important for expression of the functional conformation of this protein. We report here the localization of this Mg2+-specific binding site. We prepared three Gla-containing fragments of bovine factor IX, namely GlaEGF(NC) (residues 1-144+286-296), GlaEGF(N) (1-83) and the Gla domain peptide (1-46). Fragments GlaEGF(NC) and GlaEGF(N) retained the ability to undergo a conformational change upon binding of Mg2+ ions in the presence of excess Ca2+ ions. This change could be detected by a conformation-specific antibody. Furthermore, the Gla domain peptide was capable of binding Mg2+ ions, as determined by the metal ion-induced quenching of the intrinsic fluorescence. It appears that the (Mg2+)-specific binding site of factor IX is located in the N-terminal Gla domain.
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Surface-dependent reactions of the vitamin K-dependent enzyme complexes
KG Mann, ME Nesheim, W R Church et al. · Blood · 1990 · 857 citations · Full text
Characterization of a cDNA coding for human factor VII.
F S Hagen, C. Gray, Patrick J. O’Hara et al. · Proceedings of the National Academy of Sciences · 1986 · 452 citations · Full text