Molecular dynamics techniques can help unravel the functions of biomolecules in many ways. In this talk, I will describe how we discovered a completely new allosteric binding site in a protein family called 14-3-3. This protein family is involved in a fundamental mechanism of protein phosphorylation, a mechanism used in eukaryotic cells to activate or inactivate thousands of proteins.
Using molecular dynamics, we were able to discover the allosteric site, find and improve an active agent for this site, and describe the subsequent step after binding to the final conformational change in 14-3-3 that closes (and inactivates) the protein.