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Key Factors Regulating the Interdomain Dynamics May Contribute to the Assembly of ASC
Tongtong Li1, Laura I Gil Pineda1,2, Amy O Stevens1
1Department of Chemistry & Chemical Biology, The University of New Mexico, Albuquerque, NM 87131, USA.
Biology
|June 28, 2023
Summary
The ASC protein linker
Area of Science:
- Immunology
- Molecular Biology
- Biochemistry
Background:
- The ASC protein, comprising PYD and CARD domains, has a dynamic feature whose molecular basis is unclear.
- Understanding ASC's dynamics is crucial for inflammasome assembly and immune signaling.
Purpose of the Study:
- To investigate the role of the linker in ASC's interdomain dynamics.
- To elucidate the molecular mechanisms governing ASC monomer flexibility.
Main Methods:
- Utilized all-atom molecular dynamics simulations.
- Performed principal component analysis (PCA) and CARD spatial restraint analysis.
Main Results:
- The flexible linker facilitates interdomain dynamics and rotation.
- Linker structure, influenced by N-terminal residues and prolines, impacts domain accessibility.
- Specific structural preferences limit PYD-CARD interactions.
Conclusions:
- The semi-flexible linker is key to ASC's functionally relevant interdomain dynamics.
- Linker-induced dynamics may enhance PYD self-assembly and inflammasome complex formation.
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