Solution structure of the calmodulin-like C-terminal domain of Entamoeba α-actinin2
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
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.
a-actinin, structure, Entamoeba
Research subject Biochemistry; biological chemistry
IdentifiersURN: urn:nbn:se:umu:diva-118703DOI: 10.1002/prot.24992ISI: 000373352700005PubMedID: 26800385OAI: oai:DiVA.org:umu-118703DiVA: diva2:915275
FunderCarl Tryggers foundation