Allosteric pathways in imidazole glycerol phosphate synthase

摘要

Allostery is a fundamental property that allows the regulation of function and dynamic adaptability of enzymes and proteins. Gaining a detailed understanding of allosteric mechanisms would provide more precise control of enzyme function and roadmaps for the expansion of drug discovery beyond the active site responsible for catalytic activity. Here, we combine molecular dynamics (MD) simulations, nuclear magnetic resonance (NMR), and correlation analysis of protein motions based on network theory methods (i.e., the studies of graphs as a representation of relations between discrete objects such as the amino acid residues in proteins) and elucidate the allosteric mechanism of the enzyme imidazole glycerol phosphate synthase (IGPS) from the thermophile Thermotoga maritima.