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; Edward T Olejniczak

doi:10.1110/ps.072928007

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

Journal article

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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

Protein science, Vol.16(11), pp.2502-2509

11/2007

DOI: 10.1110/ps.072928007

PMCID: PMC2211699

PMID: 17962406

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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.

Amino Acid Sequence

Calcium - chemistry

Calcium - metabolism

Circular Dichroism

Dimerization

Escherichia coli - metabolism

Humans

Kv Channel-Interacting Proteins - chemistry

Magnetic Resonance Spectroscopy - methods

Models, Molecular

Molecular Conformation

Molecular Sequence Data

Potassium Channels - chemistry

Protein Conformation

Protein Structure, Secondary

Protein Structure, Tertiary

Details

Title: Subtitle: Solution structure and calcium-binding properties of EF-hands 3 and 4 of calsenilin
Creators: Liping Yu - Abbott
Chaohong Sun - Abbott
Renaldo Mendoza - Abbott
Jie Wang - Abbott
Edmund D Matayoshi - Abbott
Eric Hebert - Abbott
Ana Pereda-Lopez
Philip J Hajduk - Abbott
Edward T Olejniczak - Abbott
Resource Type: Journal article
Publication Details: Protein science, Vol.16(11), pp.2502-2509
DOI: 10.1110/ps.072928007
PMID: 17962406
PMCID: PMC2211699
ISSN: 0961-8368
eISSN: 1469-896X
Language: English
Date published: 11/2007
Academic Unit: Biochemistry and Molecular Biology; Medicine Administration
Record Identifier: 9984627341202771

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