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Solution structure of the calmodulin-like C-terminal domain of Entamoeba α-actinin2
Swedish NMR Centre at the University of Gothenburg.
Swedish NMR Centre at the University of Gothenburg.
Swedish NMR Centre at the University of Gothenburg.
Umeå University, Faculty of Science and Technology, Department of Chemistry.
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2016 (English)In: Proteins: Structure, Function, and Genetics, ISSN 0887-3585, E-ISSN 1097-0134, Vol. 84, no 4, 461-466 p.Article in journal (Refereed) Published
Abstract [en]

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 stru-ture ensemble of the apo form shows two lobes, that both resemble other pairs of calcium-binding EF-hand motifs, connected with a mobile linker.

Place, publisher, year, edition, pages
Wiley-Blackwell, 2016. Vol. 84, no 4, 461-466 p.
Keyword [en]
a-actinin, structure, Entamoeba
National Category
Structural Biology
Research subject
Biochemistry; biological chemistry
URN: urn:nbn:se:umu:diva-118703DOI: 10.1002/prot.24992ISI: 000373352700005PubMedID: 26800385OAI: diva2:915275
Carl Tryggers foundation
Available from: 2016-03-29 Created: 2016-03-29 Last updated: 2016-05-13Bibliographically approved

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