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

Proteins
Göran KarlssonLars Backman

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 α-actinin has been implied in several important cellular processes. In Entamoeba histolytica, the etiological agent of human amoebiasis, α-actinin is believed to be required for infection. To better understand the role of α-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.

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Citations

Mar 17, 2019·Cellular and Molecular Life Sciences : CMLS·Antonio VillaloboMartin W Berchtold
Aug 28, 2020·Proceedings of the National Academy of Sciences of the United States of America·Nikos PinotsisKristina Djinovic-Carugo

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