title: A minimal model of protein-protein binding affinities.
abstract: A minimal model of protein-protein binding affinity that takes into account only two structural features of the complex, the size of its interface, and the amplitude of the conformation change between the free and bound subunits, is tested on the 144 complexes of a structure-affinity benchmark. It yields Kd values that are within two orders of magnitude of the experiment for 67% of the complexes, within three orders for 88%, and fails on 12%, which display either large conformation changes, or a very high or a low affinity. The minimal model lacks the specificity and accuracy needed to make useful affinity predictions, but it should help in assessing the added value of parameters used by more elaborate models, and set a baseline for evaluating their performances.
authors.affiliation: IBBMC, CNRS UMR 8619, Université Paris-Sud 11, Orsay, France.
authors.forename: Joël
authors.initials: J
authors.lastname: Janin
mesh_terms: D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D013816:Thermodynamics
chemical_list: D011506:Proteins
keywords: binding energy; binding specificity; conformation change; interface area; protein-protein interaction