2E6W

Solution structure and calcium binding properties of EF-hands 3 and 4 of calsenilin

2E6W の概要

• エントリーDOI: 10.2210/pdb2e6w/pdb
• 分子名称: Calsenilin, CALCIUM ION (2 entities in total)
• 機能のキーワード: calcium-bound form, metal binding protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: Q9Y2W7
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11888.62

構造登録者

Yu, L.,Sun, C.,Mendoza, R.,Hebert, E.,Pereda-Lopez, A.,Hajduk, P.J.,Olejniczak, E.T. (登録日: 2007-01-05, 公開日: 2007-11-27, 最終更新日: 2024-05-29)

主引用文献

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

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: 17962406
DOI: 10.1110/ps.072928007

実験手法

SOLUTION NMR