All-Atom Simulations Uncover Structural and Dynamical Differences Between Open and Closed Forms of Human STING in Membrane System

Authors

Haley Pfeifer, Fort Hays State UniversityFollow
Lyly Le, Fort Hays State UniversityFollow

Award Level

3rd Place - Empirical Undergraduate

Classification

Empirical Undergraduate

Abstract

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.

Faculty Advisor

Dr. Masakatsu Watanabe

Department/Program

KAMS

Submission Type

in-person poster

DOI

10.58809/QUOO9824

Date

4-20-2022

Rights

Copyright the Author(s)

Comments

For questions contact ScholarsRepository@fhsu.edu

Recommended Citation

Pfeifer, Haley and Le, Lyly (2022) "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.
DOI: 10.58809/QUOO9824
Available at: https://scholars.fhsu.edu/sacad/vol2022/iss2022/30