Simulation data from the publication "Two cooperative lipid binding sites within the pleckstrin homology domain are necessary for AKT binding and stabilisation to the plasma membrane"

A repository of simulation data from the publication "Two cooperative lipid binding sites within the pleckstrin homology domain are necessary for AKT binding and stabilisation to the plasma membrane". Here we provide new molecular insight into the first step of AKT activation where AKT binds to the plasma membrane and its orientation is stabilised in a bilayer with lateral heterogeneity (Lo-Ld phase coexistence). We have applied coarse-grained and atomistic molecular simulations and molecular and cell biology approaches and demonstrate that AKT recruitment to the membrane occurs via a secondary binding site in the AKT Pleckstrin Homology domain that acts cooperatively with the known canonical binding site. We showed that disrupting either the canonical or secondary binding sites the membrane localisation and AKT activity is attenuated. Given the precision with which we have identified the protein-lipid interactions, the study offers new directions for AKT-targeted therapy and for testing small molecules to target these specific amino acid-PIP molecular bonds.

This dataset contains:
- DATASET 1: coarse-grained MD simulation data for the binding of the WT AKT-PH to a model membrane
- DATASET 2: coarse-grained MD simulation data for the binding of the mut1 AKT-PH to a model membrane
- DATASET 3: coarse-grained MD simulation data for the binding of the mut2 AKT-PH to a model membrane
- DATASET 4: coarse-grained MD simulation data for the binding of the mut3 AKT-PH to a model membrane
- DATASET 5: coarse-grained MD simulation data for the binding of the WT AKT-PH to a model membrane without PIP lipids
- DATASET 6: atomistic MD simulation data for the binding of the WT AKT-PH to a model membrane.