3rd Place - Empirical Undergraduate
Recent studies have shown that the stimulator of interferon gene (STING) protein plays a central role in the immune system by facilitating the production of Type I interferons in cells. The STING signaling pathway is also a prominent activator of cancer-killing T cells that initiates a powerful adaptive immune response. Since biomolecular signaling pathways are complicated and not easily identified through traditional experiments, increasing molecular dynamics (MD) capabilities provide powerful new scientific tools for decoding the pathways. We used MD simulations to study these biological pathways’ structural and dynamical responses of the full-length human STING proteins. Specifically, we investigated ligand-bound closed and ligand-unbound open forms of STING in the membrane system by comparing their conformational and dynamical differences. Our research provides clues for understanding the mechanism of the STING signaling pathway by uncovering some detailed insights for the examined systems.
Dr. Masakatsu Watanabe
Copyright the Author(s)
Pfeifer, Haley and Le, Lyly
"All-Atom Simulations Uncover Structural and Dynamical Differences Between Open and Closed Forms of Human STING in Membrane System,"
SACAD: John Heinrichs Scholarly and Creative Activity Days: Vol. 2022, Article 30.
Available at: https://scholars.fhsu.edu/sacad/vol2022/iss2022/30