Molecular dynamics study of interactions between polymorphic actin filaments and gelsolin segment-1.

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ID: 42202
2019
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Abstract
The assembly of protein actin into double-helical filaments promotes many eukaryotic cellular processes that are regulated by actin binding proteins (ABPs). Actin filaments can adopt multiple conformations, known as structural polymorphism, which possibly influences the interaction between filaments and ABPs. Gelsolin is a Ca -regulated ABP that severs and caps actin filaments. Gelsolin binding modulates filament structure; however, it is not known how polymorphic actin filament structures influence an interaction of gelsolin S1 with the barbed-end of filament. Herein, we investigated how polymorphic structures of actin filaments affect the interactions near interfaces between the gelsolin segment 1 (S1) domain and the filament barbed-end. Using all-atom molecular dynamics simulations, we demonstrate that different tilted states of subunits modulate gelsolin S1 interactions with the barbed-end of polymorphic filaments. Hydrogen bonding and interaction energy at the filament-gelsolin S1 interface indicate distinct conformations of filament barbed ends resulting in different interactions of gelsolin S1. This study demonstrates that filament's structural multiplicity plays important roles in the interactions of actin with ABPs. This article is protected by copyright. All rights reserved.
Reference Key
lee2019molecularproteins Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Lee, Myeongsang;Kang, Ellen Hyeran;
Journal Proteins
Year 2019
DOI
10.1002/prot.25813
URL
Keywords Keywords not found

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