2E6W
Solution structure and calcium binding properties of EF-hands 3 and 4 of calsenilin
Summary for 2E6W
| Entry DOI | 10.2210/pdb2e6w/pdb |
| Descriptor | Calsenilin, CALCIUM ION (2 entities in total) |
| Functional Keywords | calcium-bound form, metal binding protein |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm: Q9Y2W7 |
| Total number of polymer chains | 1 |
| Total formula weight | 11888.62 |
| Authors | Yu, L.,Sun, C.,Mendoza, R.,Hebert, E.,Pereda-Lopez, A.,Hajduk, P.J.,Olejniczak, E.T. (deposition date: 2007-01-05, release date: 2007-11-27, Last modification date: 2024-05-29) |
| Primary citation | Yu, L.,Sun, C.,Mendoza, R.,Wang, J.,Matayoshi, E.D.,Hebert, E.,Pereda-Lopez, A.,Hajduk, P.J.,Olejniczak, E.T. Solution structure and calcium-binding properties of EF-hands 3 and 4 of calsenilin. Protein Sci., 16:2502-2509, 2007 Cited by PubMed Abstract: Calsenilin is a member of the recoverin branch of the EF-hand superfamily that is reported to interact with presenilins, regulate prodynorphin gene expression, modulate voltage-gated Kv4 potassium channel function, and bind to neurotoxins. Calsenilin is a Ca+2-binding protein and plays an important role in calcium signaling. Despite its importance in numerous neurological functions, the structure of this protein has not been reported. In the absence of Ca+2, the protein has limited spectral resolution that increases upon the addition of Ca+2. Here, we describe the three-dimensional solution structure of EF-hands 3 and 4 of calsenilin in the Ca+2-bound form. The Ca+2-bound structure consists of five alpha-helices and one two-stranded antiparallel beta-sheet. The long loop that connects EF hands 3 and 4 is highly disordered in solution. In addition to its structural effects, Ca+2 binding also increases the protein's propensity to dimerize. These changes in structure and oligomerization state induced upon Ca+2 binding may play important roles in molecular recognition during calcium signaling. PubMed: 17962406DOI: 10.1110/ps.072928007 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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