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Solution structure and calcium‐binding properties of EF‐hands 3 and 4 of calsenilin
Author(s) -
Yu Liping,
Sun Chaohong,
Mendoza Renaldo,
Wang Jie,
Matayoshi Edmund D.,
Hebert Eric,
PeredaLopez Ana,
Hajduk Philip J.,
Olejniczak Edward T.
Publication year - 2007
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.072928007
Subject(s) - antiparallel (mathematics) , ef hand , calcium binding protein , calmodulin , biophysics , chemistry , recoverin , protein structure , calcium signaling , calcium , crystallography , biochemistry , signal transduction , biology , enzyme , physics , retinal , organic chemistry , quantum mechanics , magnetic field , rhodopsin
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 α‐helices and one two‐stranded antiparallel β‐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.