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

Karlsson G, Persson C, Mayzel M, Hedenström M, Backman L

Proteins 84 (4) 461-466 [2016-04-00; online 2016-02-05]

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.

Swedish NMR Centre (SNC) [Collaborative]

QC bibliography QC xrefs

PubMed 26800385

DOI 10.1002/prot.24992

Crossref 10.1002/prot.24992