title: Protein-protein interaction site mapping using NMR-detected mutational scanning.
abstract: We demonstrate a novel NMR method for the mapping of protein-protein interaction sites. In our approach protein-protein binding sites are mapped by competition binding experiments using indirect NMR reporter technology and Ala positional scanning. The methodology provides high sensitivity, ease of implementation and high-throughput capabilities. The feasibility of the technique is demonstrated with an application to the beta-Catenin/Tcf4 complex.
authors: Department of Biomolecular Structural Chemistry, Max F. Perutz Laboratories, University of Vienna, Vienna, 1030, Austria.
authors: Bettina
authors: B
authors: Baminger
authors: Martin L
authors: ML
authors: Ludwiczek
authors: Georg
authors: G
authors: Kontaxis
authors: Stefan
authors: S
authors: Knapp
authors: Robert
authors: R
authors: Konrat
mesh_terms: D001667:Binding, Competitive; D006801:Humans; D008024:Ligands; D008958:Models, Molecular; D009154:Mutation / Q000235:genetics*; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D025941:Protein Interaction Mapping / Q000379:methods*; D015203:Reproducibility of Results; D051820:TCF Transcription Factors / Q000378:metabolism; D058118:Transcription Factor 7-Like 2 Protein; D051176:beta Catenin / Q000378:metabolism
chemical_list: D008024:Ligands; D051820:TCF Transcription Factors; C544894:TCF7L2 protein, human; D058118:Transcription Factor 7-Like 2 Protein; D051176:beta Catenin