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| 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 |
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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