Article
Synergistic Allosteric Mechanism of Fructose-1,6-bisphosphate and Serine for Pyruvate Kinase M2 via Dynamics Fluctuation Network Analysis.
Journal of chemical information and modeling - 27 Jun 2016
Yang Jingxu, Liu Hao, Liu Xiaorui, Gu Chengbo, Luo Ray, Chen Hai-Feng
Abstract excerpt
Pyruvate kinase M2 (PKM2) plays a key role in tumor metabolism and regulates the rate-limiting final step of glycolysis. In tumor cells, there are two allosteric effectors for PKM2: fructose-1,6-bisphosphate (FBP) and serine. However, the relationship between FBP and serine for allosteric regulation of PKM2 is unknown. Here we constructed residue/residue fluctuation correlation network based on all-atom molecular...
Topics
- Allosteric Regulation
- Drug Synergism
- Enzyme Stability
- Fructosediphosphates
- Molecular Dynamics Simulation
- Mutation
- Protein Conformation
- Pyruvate Kinase
- Serine
- Thermodynamics