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2e6w
From Proteopedia
| 2e6w, 1 NMR models () | |||||||||
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| Ligands: | |||||||||
| Gene: | DREAM, KCHIP3 (Homo sapiens) | ||||||||
| Domains: | EFh | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Solution structure and calcium binding properties of EF-hands 3 and 4 of calsenilin
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.
Solution structure and calcium-binding properties of EF-hands 3 and 4 of calsenilin., Yu L, Sun C, Mendoza R, Wang J, Matayoshi ED, Hebert E, Pereda-Lopez A, Hajduk PJ, Olejniczak ET, Protein Sci. 2007 Nov;16(11):2502-9. PMID:17962406
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
2E6W is a 1 chain structure of sequence from Homo sapiens. Full experimental information is available from OCA.
Reference
- Yu L, Sun C, Mendoza R, Wang J, Matayoshi ED, Hebert E, Pereda-Lopez A, Hajduk PJ, Olejniczak ET. Solution structure and calcium-binding properties of EF-hands 3 and 4 of calsenilin. Protein Sci. 2007 Nov;16(11):2502-9. PMID:17962406
Page seeded by OCA on Mon Feb 16 12:43:38 2009
