Table Info

Table 3.

Summary of result analysis

Feature	Normal cell HER2/ERBB2	Cancer cell HER2/ERBB2
Number of dimerized structures obtained	12	15
PIPER pose energy score (best docking score)	–133.7 (No score above –900)	–1,238.94 (Scores above –900)
Number of interacting residues	12	165
Stability of homodimers	No stable dimer found	Stable dimer structures obtained
Interaction analysis in Schrödinger	Unable to perform due to weak interactions	Conducted successfully, showing strong to very strong interactions
Sequence identity (BLASTP)	-	99% similarity with normal HER2/ERBB2
Sequence identity (EMBOSS WATER)	-	99.6% similarity with normal HER2/ERBB2
Secondary structure comparison (PSIPRED)	-	Shift in loops, helices, and sheets observed compared to normal HER2/ERBB2
3D structure comparison (Chimera)	-	Slight difference and shift in protein folding compared to normal HER2/ERBB2

Supplementary materials

The supplementary figures for this article are available at: https://www.explorationpub.com/uploads/Article/file/1001237_sup_1.pdf.

Declarations

Acknowledgments

We thank Hybrinomics Life Science & Diagnostics LLP, for their willingness to allow public access to their web services, particularly Schrödinger software.

Author contributions

JS: Methodology, Investigation, Writing—original draft. PM: Conceptualization, Methodology, Investigation, Supervision, Writing—review & editing. HV: Formal analysis, Writing—review & editing. All authors read and approved the submitted version.

Conflicts of interest

The authors declare that they have no conflicts of interest.

Ethical approval

Not applicable.

Consent to participate

Not applicable.

Consent to publication

Not applicable.

Availability of data and materials

The raw data supporting the conclusions of this manuscript will be made available by the authors, without undue reservation, to any qualified researcher.

Funding

Not applicable.

Copyright

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