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Related Experiment Video

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Evolution of Thyroglobulin Loop Kinetics in EpCAM.

Serena H Chen1, David R Bell2

  • 1Oak Ridge National Laboratory, Computational Sciences and Engineering Division, Oak Ridge, TN 37830, USA.

Life (Basel, Switzerland)
|September 28, 2021
PubMed
Summary
This summary is machine-generated.

The Epithelial cell-activating molecule (EpCAM) TY loop remains dynamic across species. Fish EpCAM shows unique binding patterns compared to other organisms, influenced by its TY loop sequence.

Keywords:
EpCAMevolutionkineticsmolecular dynamics simulationthyroglobulin loop

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Epithelial cell-activating molecule (EpCAM) is a crucial cancer biomarker and therapeutic target due to its overexpression in epithelial cancers.
  • EpCAM is a type I transmembrane protein that dimerizes via its extracellular thyroglobulin type-1A-like domain (TYD).
  • The EpCAM TY loop within the TYD exhibits dynamic behavior and reversible binding in its monomeric state.

Purpose of the Study:

  • To investigate the evolutionary conservation and species-specific dynamics of the EpCAM TY loop.
  • To identify potential binding sites for the EpCAM TY loop beyond the TYD.
  • To understand the structural basis for differential EpCAM binding patterns across species.

Main Methods:

  • Utilized over 17 microseconds of all-atom molecular dynamics simulations.
  • Analyzed EpCAM TY loop kinetics in five species: human, mouse, chicken, frog, and fish.
  • Calculated dissociation rate constants to determine binding affinities.

Main Results:

  • The EpCAM TY loop demonstrates conserved dynamic behavior across all studied species.
  • A second binding site for the TY loop was identified in the C-terminal domain (CTD).
  • Fish EpCAM exhibits distinct binding kinetics, with comparable affinity for both TYD and CTD sites, unlike other species that preferentially bind the TYD.

Conclusions:

  • The EpCAM TY loop's structural dynamics are evolutionarily conserved.
  • The sequence of the TY loop significantly influences its dynamic behavior and binding preferences.
  • Findings offer insights into EpCAM's structural dynamics and physiological roles, with implications for cancer therapy.