1CMG
NMR SOLUTION STRUCTURE OF CALCIUM-LOADED CALMODULIN CARBOXY-TERMINAL DOMAIN
Summary for 1CMG
| Entry DOI | 10.2210/pdb1cmg/pdb |
| Descriptor | CALMODULIN (VERTEBRATE) (1 entity in total) |
| Functional Keywords | calcium-binding protein |
| Biological source | Bos taurus (cattle) |
| Cellular location | Cytoplasm: P62157 |
| Total number of polymer chains | 1 |
| Total formula weight | 8416.20 |
| Authors | Evenas, J.,Finn, B.E.,Drakenberg, T.,Waltho, J.P.,Thulin, E.,Forsen, S. (deposition date: 1995-07-19, release date: 1995-12-07, Last modification date: 2024-05-22) |
| Primary citation | Finn, B.E.,Evenas, J.,Drakenberg, T.,Waltho, J.P.,Thulin, E.,Forsen, S. Calcium-induced structural changes and domain autonomy in calmodulin. Nat.Struct.Biol., 2:777-783, 1995 Cited by PubMed Abstract: We have determined the solution structures of the apo and (Ca2+)2 forms of the carboxy-terminal domain of calmodulin using multidimensional heteronuclear nuclear magnetic resonance spectroscopy. The results show that both forms adopt well-defined structures with essentially equal secondary structure. A comparison of the structures of the two forms shows that Ca2+ binding causes major rearrangements of the secondary structure elements with changes in inter-residue distances of up to 15 A and exposure of the hydrophobic interior of the four-helix bundle. Comparisons with previously determined high-resolution X-ray structures and models of calmodulin indicate that this domain is structurally autonomous. PubMed: 7552749DOI: 10.1038/nsb0995-777 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
