Network representation of protein interactions-Experimental results

Abstract : A graph theoretical analysis of nuclear magnetic resonance (NMR) data of six different protein interactions has been presented. The representation of the protein interaction data as a graph or network reveals that all of the studied interactions are based on a common functional concept. They all involve a single densely packed hub of functionally correlated residues that mediate the ligand binding events. This is found independent of the kind of protein (folded or unfolded) or ligand (protein, polymer or small molecule). Furthermore, the power of the graph analysis is demonstrated at the examples of the Calmodulin (CaM)/Calcium and the Cold Shock Protein A (CspA)/RNA interaction. The presented approach enables the precise determination of multiple binding sites for the respective ligand molecules.
Type de document :
Article dans une revue
Protein Science, Wiley, 2016, 25 (9), pp.1628 - 1636. 〈10.1002/pro.2964〉
Domaine :
Liste complète des métadonnées

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Dennis Kurzbach, Andrea Flamm, Tomáš Sára. Network representation of protein interactions-Experimental results. Protein Science, Wiley, 2016, 25 (9), pp.1628 - 1636. 〈10.1002/pro.2964〉. 〈hal-01596094〉



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