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Solution structure of the calmodulin-like C-terminal domain of Entamoeba-actinin2

Journal article
Authors B Göran Karlsson
Cecilia Persson
Maxim Mayzel
M. Hedenstrom
L. Backman
Published in Proteins-Structure Function and Bioinformatics
Volume 84
Issue 4
Pages 461-466
ISSN 0887-3585
Publication year 2016
Published at Swedish NMR Centre at Göteborg University
Pages 461-466
Language en
Links dx.doi.org/10.1002/prot.24992
Keywords alpha-actinin, structure, calcium-binding proteins, alpha-actinin gene, skeletal-muscle, histolytica, system, evolution, spectrin, cloning, lectin, model, Biochemistry & Molecular Biology
Subject categories Chemical Sciences

Abstract

Cell motility is dependent on a dynamic meshwork of actin filaments that is remodelled continuously. A large number of associated proteins that are severs, cross-links, or caps the filament ends have been identified and the actin cross-linker -actinin has been implied in several important cellular processes. In Entamoeba histolytica, the etiological agent of human amoebiasis, -actinin is believed to be required for infection. To better understand the role of -actinin in the infectious process we have determined the solution structure of the C-terminal calmodulin-like domain using NMR. The final structure ensemble of the apo form shows two lobes, that both resemble other pairs of calcium-binding EF-hand motifs, connected with a mobile linker. Proteins 2016; 84:461-466.

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