What question did this study set out to answer?

The aim is to understand the structural and dynamic aspects of the PODXL–Ezrin interaction, particularly in the context of cancer progression.

February 5, 2026Journal of XenobioticsOpen Access

Structural and Dynamic Insights into Podocalyxin–Ezrin Interaction as a Target in Cancer Progression

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Integrated computational methods reveal PODXL–Ezrin interaction dynamics, suggesting new cancer treatment strategies.

The aim is to understand the structural and dynamic aspects of the PODXL–Ezrin interaction, particularly in the context of cancer progression.
Combined protein-protein docking and molecular dynamics simulations to analyze PODXL and Ezrin interactions.
Modelled complexes using AlphaFold-predicted structures to study binding dynamics.
Investigated the impact of the R495W missense mutation on the PODXL–Ezrin interface.
The R495W mutation results in increased intramolecular distance affecting Ezrin activation.
Molecular dynamics simulations reveal enhanced rigidity in the R495W mutant, suggesting a potential 'locked' active state.
Identified NSC305787 as a selective destabiliser for the R495W mutant, with implications for drug development.

Milutinovic et al. (2026) studied this question.

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