Protein & Peptide Letters

Prof. Ben M. Dunn  
Department of Biochemistry and Molecular Biology
University of Florida
College of Medicine
P.O. Box 100245
Gainesville, FL
USA
Email: bdunn@ufl.edu

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Functional and Structural Analysis of the Conserved EFhd2 Protein

Author(s): Yancy Ferrer-Acosta, Eva N. Rodriguez Cruz, Ana del C. Vaquer and Irving E. Vega

Affiliation: Department of Biology, University of Puerto Rico-Rio Piedras Campus, Julio García Diaz Bldg. #120, San Juan, PR 00931, USA.

Keywords: EFHD2, calcium binding, EF-hand domain, coil-coiled domain, tau-associated protein, secondary structure

Abstract:

EFhd2 is a novel protein conserved from C. elegans to H. sapiens. This novel protein was originally identified in cells of the immune and central nervous systems. However, it is most abundant in the central nervous system, where it has been found associated with pathological forms of the microtubule-associated protein tau. The physiological or pathological roles of EFhd2 are poorly understood. In this study, a functional and structural analysis was carried to characterize the molecular requirements for EFhd2’s calcium binding activity. The results showed that mutations of a conserved aspartate on either EF-hand motif disrupted the calcium binding activity, indicating that these motifs work in pair as a functional calcium binding domain. Furthermore, characterization of an identified single-nucleotide polymorphisms (SNP) that introduced a missense mutation indicates the importance of a conserved phenylalanine on EFhd2 calcium binding activity. Structural analysis revealed that EFhd2 is predominantly composed of alpha helix and random coil structures and that this novel protein is thermostable. EFhd2’s thermo stability depends on its N-terminus. In the absence of the N-terminus, calcium binding restored EFhd2’s thermal stability. Overall, these studies contribute to our understanding on EFhd2 functional and structural properties, and introduce it into the family of canonical EF-hand domain containing proteins.

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Article Details

VOLUME: 20
ISSUE: 5
Page: [573 - 583]
Pages: 11
DOI: 10.2174/0929866511320050011