Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
6877734 | Journal of Molecular Graphics and Modelling | 2014 | 11 Pages |
Abstract
- MDs were done to simulate the binding modes of 3 allosteric inhibitors with PKBα.
- The structure requirements were analyzed for allosteric inhibitor binding to PKBα.
- The free energy calculations mirrored the allosteric inhibitors' bioactivities.
- The possible structural mechanism of PKBα inhibition was explored theoretically.
Keywords
PI3KRMSDMM/GBSASMDPDK1root-mean-square deviationsMM/PBSAPKB/AKTBinding free energyMolecular dynamicsSteered Molecular DynamicsBinding mechanismMolecular dynamics simulationphosphatase and tensin homologAllosteric inhibitorMolecular Mechanics/Generalized Born Surface AreaPleckstrin Homologyprotein kinase BPten
Related Topics
Physical Sciences and Engineering
Chemistry
Physical and Theoretical Chemistry
Authors
Shi-Feng Chen, Yang Cao, Shuang Han, Jian-Zhong Chen,