Premium
Network representation of protein interactions—Experimental results
Author(s) -
Kurzbach Dennis,
Flamm Andrea G.,
Sára Tomáš
Publication year - 2016
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.2964
Subject(s) - interaction network , ligand (biochemistry) , calmodulin , chemistry , protein–protein interaction , graph , protein ligand , representation (politics) , computational biology , small molecule , biological system , biophysics , physics , computer science , biology , biochemistry , theoretical computer science , gene , receptor , politics , political science , law , enzyme
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.