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Cocktail and Poster Display session

46P - Dynamics of ROS1 kinase binding: Insights into DFG-out tyrosine kinase inhibitors and effects of allosteric-pocket mutations

Date

26 Feb 2024

Session

Cocktail and Poster Display session

Topics

Targeted Therapy

Tumour Site

Presenters

Farhan Haq

Citation

Annals of Oncology (2024) 9 (suppl_1): 1-11. 10.1016/esmoop/esmoop102271

Authors

F.U. Haq1, K. Op de Beeck1, G. Van Camp1, G. Vandeweyer2

Author affiliations

  • 1 Medical Genetics, University of Antwerp, 2650 - Edegem/BE
  • 2 Medical Genetics, Antwerp University Hospital, 2650 - Edegem/BE

Resources

This content is available to ESMO members and event participants.

Abstract 46P

Background

The oncogenic potential of c-ros oncogene 1 (ROS1) has been established recently, especially in rare non-small cell lung cancer (NSCLC) patients with hallmark ROS1 gene-fusions. The fused gene partners often dictate the localisation whereas the conserved kinase domain ensures a constitutively activated kinase. Personalized, anti-cancer therapies using tyrosine kinase inhibitors (TKIs) have achieved success in the past for related kinase targets, including epidermal growth factor receptor (EGFR) and anaplastic lymphoma kinase (ALK). This targeted approach has been translated to ROS1, but the overall success is greatly affected by kinase domain resistance mutations.

Methods

Due to lack of ROS1 experimental structures in the inactive (DFG-out) state, we employ homology modelling using a related template, c-ABL kinase structure (PDB entry 1IEP), to model inactive ROS1 wild-type (WT) and mutant structures. These models are then subjected to molecular docking to generate protein-ligand complexes with type 2 TKIs. Obtained complexes are evaluated by all-atom molecular dynamic (MD) simulations.

Results

The ROS1 DFG-out state models for the WT and two mutants, F2004C and F2004V (in proximity of αC-helix), were successfully evaluated using key features distinguishing active and inactive states. The starting models showed clear differences for selected distance and angle-based calculations. This provided the structural basis to study type 2 TKIs bound to the inactive ROS1 receptor and to evaluate the effect of resistance mutations in the absence of experimental structural information.

Conclusions

The findings from this computational exploration contribute valuable insights into structural dynamics of the ROS1 kinase domain, the impact of point mutations near key regulatory regions, and protein-ligand interaction profiles with inactive-kinase specific TKIs.

Clinical trial identification

Editorial acknowledgement

Legal entity responsible for the study

The authors.

Funding

Fonds Wetenschappelijk Onderzoek - Vlaanderen; Stichting Kom Op Tegen Kanker.

Disclosure

All authors have declared no conflicts of interest.

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