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PIK3CA somatic mutations in breast cancer: Mechanistic insights from Langevin dynamics simulations
Parminder K Mankoo1, Saraswati Sukumar, Rachel Karchin
1Department of Biomedical Engineering and Institute for Computational Medicine, Johns Hopkins University, Baltimore, Maryland 21218, USA.
Abstract:
Somatic mutations in PIK3CA (phosphatidylinositol-3 kinase, catalytic subunit, alpha isoform) are reported in breast and other human cancers to concentrate at hotspots within its kinase and helical domains. Most of these mutations cause kinase gain of function in vitro and are associated with oncogenicity in vivo. However, little is known about the mechanisms driving tumor development. We have performed computational structural studies on a homology model of wildtype PIK3CA plus recurrent H1047R, H1047L, and P539R mutations, located in the kinase and helical domains, respectively. The time evolution of the structures show that H1047R/L mutants exhibit a larger area of the catalytic cleft between the kinase N- and C-lobes compared with the wildtype that could facilitate the entrance of substrates. This larger area might yield enhanced substrate-to-product turnover associated with oncogenicity. In addition, the H1047R/L mutants display increased kinase activation loop mobility, compared with the wildtype. The P539R mutant forms more hydrogen bonds and salt-bridge interactions than the wildtype, properties that are associated with enhanced thermostability. Mutant-specific differences in the catalytic cleft and activation loop behavior suggest that structure-based mutant-specific inhibitors can be designed for PIK3CA-positive breast cancers.
Insights
Somatic mutations in PIK3CA drive cancer by altering its structure and function. Computational studies reveal how specific PIK3CA mutations enhance substrate access and activity, suggesting targeted inhibitor development for PIK3CA-driven cancers.
Area of Science:
- Molecular Biology
- Cancer Genetics
- Structural Biology
Background:
- Somatic mutations in PIK3CA are prevalent in various human cancers, including breast cancer.
- Most PIK3CA mutations lead to increased kinase activity and are linked to oncogenesis.
- The precise mechanisms by which these mutations drive tumor development remain incompletely understood.
Purpose of the Study:
- To investigate the structural and dynamic consequences of recurrent PIK3CA mutations.
- To elucidate the molecular mechanisms underlying PIK3CA-mediated oncogenicity.
- To explore the potential for developing structure-based, mutant-specific inhibitors.
Main Methods:
- Computational structural studies using homology modeling of wildtype and mutant PIK3CA.
- Analysis of molecular dynamics simulations to assess structural changes and protein behavior.
- Examination of mutations at specific hotspots within the kinase and helical domains.
Main Results:
- H1047R/L PIK3CA mutants showed an enlarged catalytic cleft, potentially facilitating substrate entry and increasing turnover.
- Mutant H1047R/L exhibited enhanced activation loop mobility compared to wildtype PIK3CA.
- The P539R mutant displayed increased hydrogen bond and salt-bridge interactions, suggesting enhanced thermostability.
Conclusions:
- Mutant-specific alterations in the catalytic cleft and activation loop dynamics provide mechanistic insights into PIK3CA oncogenicity.
- These findings support the development of targeted therapies for PIK3CA-mutated cancers.
- Structure-based drug design can yield mutant-specific inhibitors for PIK3CA-positive breast cancers.
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