Directly observed hydrogen bonds at calcium-binding-sites of calmodulin in solution relate to affinity of the calcium-binding
| Autor: | Elena Atanasova, Franklyn G. Prendergast, Slobodan Macura, Nenad Juranić |
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| Rok vydání: | 2009 |
| Předmět: |
Binding Sites
Calmodulin biology Hydrogen bond Glutamate receptor Glutamic Acid chemistry.chemical_element Hydrogen Bonding Crystal structure Calcium Crystallography X-Ray Biochemistry Protein Structure Secondary Inorganic Chemistry Crystallography Lower affinity Protein structure chemistry biology.protein Animals Humans Binding site Protein Binding |
| Zdroj: | Journal of Inorganic Biochemistry. 103:1415-1418 |
| ISSN: | 0162-0134 |
| DOI: | 10.1016/j.jinorgbio.2009.08.006 |
| Popis: | Molecular tuning to calcium-binding in the EF-hand motif of holo-calmodulin was studied in solution by NMR h3JNC′ H-bond couplings. In the N-terminus lobe of holo-calmodulin, the glutamate crucial for Ca2+ coordination has network of H-bonds weaker than inferred from the X-ray crystal structure. This glutamate at position 12 appears shifted away from the Ca2+ preferred coordination, which can explain the lower affinity of the calcium-binding to the N-terminus with respect to C-terminus EF hands. |
| Databáze: | OpenAIRE |
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