ArticleBiochimica et biophysica acta. Molecular cell research2020
Multiscale simulation unravel the kinetic mechanisms of inflammasome assembly.
Article in Biochimica et biophysica acta. Molecular cell research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Dissecting the general mechanisms of protein cage self-assembly by coarse-grained simulations.Protein science : a publication of the Protein Society · 2023Article
- Protein assembly and crowding simulations.Current opinion in structural biology · 2022Review
- Computational Simulation of Holin S105 in Membrane Bilayer and Its Dimerization Through a Helix-Turn-Helix Motif.The Journal of membrane biology · 2021Article
- Understanding the impacts of cellular environments on ligand binding of membrane receptors by computational simulations.The Journal of chemical physics · 2021Article
- Understand the Functions of Scaffold Proteins in Cell Signaling by a Mesoscopic Simulation Method.Biophysical journal · 2020Article
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2 authors.
Funding
Abstract
In the innate immune system, the host defense from the invasion of external pathogens triggers the inflammatory responses. Proteins involved in the inflammatory pathways were often found to aggregate into supramolecular oligomers, called 'inflammasome', mostly through the homotypic interaction between their domains that belong to the death domain superfamily. Although much has been known about the formation of these helical molecular machineries, the detailed correlation between the dynamics of their assembly and the structure of each domain is still not well understood. Using the filament formed by the PYD domains of adaptor molecule ASC as a test system, we constructed a new multiscale simulation framework to study the kinetics of inflammasome assembly. We found that the filament assembly is a multi-step, but highly cooperative process. Moreover, there are three types of binding interfaces between domain subunits in the ASC
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