2e6w
From Proteopedia
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Solution structure and calcium binding properties of EF-hands 3 and 4 of calsenilin
Overview
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.
About this Structure
2E6W is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Wed Jan 23 11:58:00 2008
