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Protein Science (2007), 16:2502-2509. Published by Cold Spring Harbor Laboratory Press. Copyright © 2007 The Protein Society
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Solution structure and calcium-binding properties of EF-hands 3 and 4 of calsenilin

Liping Yu, Chaohong Sun, Renaldo Mendoza, Jie Wang, Edmund D. Matayoshi, Eric Hebert, Ana Pereda-Lopez, Philip J. Hajduk, and Edward T. Olejniczak

Pharmaceutical Discovery Division, Global Pharmaceutical Research and Development, Abbott Laboratories, Abbott Park, Illinois 60064-6098, USA

(RECEIVED April 9, 2007; FINAL REVISION July 18, 2007; ACCEPTED July 18, 2007)

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.

Keywords: calsenilin; DREAM; KChIP3; calcium-binding protein; EF-hands; NMR structure


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