Network representation of protein interactions-Experimental results.
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.
Departement de Chimie, Ecole Normale Superieure, PSL Research University, UPMC Univ Paris 06, CNRS, Laboratoire des Biomolecules (LBM), 24 rue Lhomond, 75005, Paris, France.
Dennis
D
Kurzbach
Department for Structural and Computational Biology, University of Vienna, Campus Vienna BioCenter 5, Vienna, 1030, Austria.
Andrea G
AG
Flamm
Department for Structural and Computational Biology, University of Vienna, Campus Vienna BioCenter 5, Vienna, 1030, Austria.
Tomáš
T
Sára
D002118:Calcium / Q000737:chemistry*; D002147:Calmodulin / Q000737:chemistry*; D057773:Cold Shock Proteins and Peptides / Q000737:chemistry*; D006801:Humans; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular
D002147:Calmodulin; D057773:Cold Shock Proteins and Peptides; D002118:Calcium
chemical shift; graph theory; network description; nuclear magnetic resonance; protein interactions; relaxation