Functional characterization of Val60, a key residue involved in the membrane-oligomerization of fragaceatoxin C, an actinoporin fromActinia fragacea
| Autor: | Koldo Morante, Kouhei Tsumoto, Ana Rosa Viguera, Jose M. M. Caaveiro, Juan Manuel González-Mañas |
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| Rok vydání: | 2015 |
| Předmět: |
Circular dichroism
Molecular Sequence Data Biophysics Calorimetry Biochemistry Polymerization Residue (chemistry) Cnidarian Venoms Protein oligomerization Structural Biology Genetics Animals Amino Acid Sequence Molecular Biology Pore-forming toxins Pore-forming toxin Sequence Homology Amino Acid biology Chemistry Point mutation Lipid–protein interaction Valine Cell Biology biology.organism_classification Sea Anemones Membrane Model membranes Sphingomyelin Actinia |
| Zdroj: | FEBS Letters. 589:1840-1846 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/j.febslet.2015.06.012 |
| Popis: | Actinoporins are pore-forming toxins produced by different sea anemones that self-assemble within the membranes of their target cells and compromise their function as a permeability barrier. The recently published three-dimensional structures of two oligomeric complexes formed by fragaceatoxin C point to Val60 as a key residue involved in the oligomerization of the functional pore. To gain insight into the mechanism of toxin oligomerization, different point mutations have been introduced at this position. Functional characterization of the muteins suggests that Val60 represents a hot-spot where the introduction of mutations hinders protein assembly and reduces the overall affinity for membranes. |
| Databáze: | OpenAIRE |
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