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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Linse, S. Forsén, S. Andersson, M. Svensson, L. A. Ivarsson, I. Malmendal, A. |
| Description | Country affiliation: Sweden Author Affiliation: Andersson M ( Department of Molecular Biophysics, Lund University, Sweden.) |
| Abstract | The three-dimensional structures of the magnesium- and manganese-bound forms of calbindin D9k were determined to 1.6 A and 1.9 A resolution, respectively, using X-ray crystallography. These two structures are nearly identical but deviate significantly from both the calcium bound form and the metal ion-free (apo) form. The largest structural differences are seen in the C-terminal EF-hand, and involve changes in both metal ion coordination and helix packing. The N-terminal calcium binding site is not occupied by any metal ion in the magnesium and manganese structures, and shows little structural deviation from the apo and calcium bound forms. 1H-NMR and UV spectroscopic studies at physiological ion concentrations show that the C-terminal site of the protein is significantly populated by magnesium at resting cell calcium levels, and that there is a negative allosteric interaction between magnesium and calcium binding. Calcium binding was found to occur with positive cooperativity at physiological magnesium concentration. |
| ISSN | 09618368 |
| e-ISSN | 1469896X |
| Journal | Protein Science |
| Issue Number | 6 |
| Volume Number | 6 |
| Language | English |
| Publisher | Wiley-Blackwell (on behalf of The Protein Society) |
| Publisher Date | 1997-06-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Calcium Chemistry Magnesium S100 Calcium Binding Protein G Allosteric Regulation Calbindins Metabolism Cations, Divalent Crystallography, X-ray Magnetic Resonance Spectroscopy Models, Chemical Models, Molecular Protein Conformation Comparative Study Research Support, Non-u.s. Gov't Discipline Biochemistry |
| Content Type | Text |
| Resource Type | Article |
| Subject | Medicine Molecular Biology Biochemistry |
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