Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1316825 | Journal of Inorganic Biochemistry | 2009 | 4 Pages |
Abstract
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.
Related Topics
Physical Sciences and Engineering
Chemistry
Inorganic Chemistry
Authors
Nenad Juranić, Elena Atanasova, Slobodan Macura, Franklyn G. Prendergast,