NMR Applications for Identifying β-TrCP Protein-Ligand Interactions

Title: NMR Applications for Identifying β-TrCP Protein-Ligand Interactions

Volume: 11 Issue: 4

Author(s): J. Pons, V. Tanchou, J.-P. Girault, G. Bertho and N. Evrard-Todeschi

Affiliation:

Keywords: STD-NMR, WaterLOGSY, epitope mapping, docking, phosphorylated peptide, TrCP complex, binding fragment, protein-ligand interactions, magnetization transfer, dissociation constant, ligand competition assays, ATF4, TrCP, HSQC, MBP, NOESY, ROESY, SCF, TOCSY

Abstract: In the absence of crystallographic data, NMR has emerged as the best way to define protein-ligand interactions. Using NMR experiments based on magnetization transfer, one can sort bound from unbound molecules, estimate the dissociation constant, identify contacts implied in the binding, characterize the structure of the bound ligand and conduct ligand competition assays.

Cite this article as:

Pons J., Tanchou V., Girault J.-P., Bertho G. and Evrard-Todeschi N., NMR Applications for Identifying β-TrCP Protein-Ligand Interactions, Mini-Reviews in Medicinal Chemistry 2011; 11 (4) . https://dx.doi.org/10.2174/138955711795305344