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Modulation of post-powerstroke dynamics in myosin II by 2′-deoxy-ADP

Childers, Matthew Carter, Geeves, Michael, Daggett, Valerie, Regnier, Michael (2021) Modulation of post-powerstroke dynamics in myosin II by 2′-deoxy-ADP. Archives of Biochemistry and Biophysics, 699 . Article Number 108733. ISSN 0003-9861. (doi:10.1016/ (KAR id:86705)


Muscle myosins are molecular motors that hydrolyze ATP and generate force through coordinated interactions with actin filaments, known as cross-bridge cycling. During the cross-bridge cycle, functional sites in myosin ‘sense’ changes in interactions with actin filaments and the nucleotide binding region, resulting in allosteric transmission of information throughout the structure. We investigated whether the dynamics of the post- powerstroke state of the cross-bridge cycle are modulated in a nucleotide-dependent fashion. We compared molecular dynamics simulations of the myosin II motor domain (M) from Dictyostelium discoideum in the presence of ADP (M.ADP) versus 2′-deoxy-ADP bound myosin (M.dADP). We found that dADP was more flexible than ADP and the two nucleotides interacted with myosin in different ways. Replacement of ADP with dADP in the post- powerstroke state also altered the conformation of the actin binding region in myosin heads. Our results provide atomic level insights into allosteric communication networks in myosin that provide insight into the nucleotide- dependent dynamics of the cross-bridge cycle.

Item Type: Article
DOI/Identification number: 10.1016/
Uncontrolled keywords: Myosin, Molecular dynamics, simulation, Allostery
Subjects: Q Science > QD Chemistry > QD431 Organic Chemistry- Biochemistry- Proteins, peptides, amino acids
Divisions: Divisions > Division of Natural Sciences > Biosciences
Funders: Agency for Mobility and EU Programmes (
Depositing User: Michael Geeves
Date Deposited: 21 Feb 2021 12:14 UTC
Last Modified: 04 Mar 2024 16:00 UTC
Resource URI: (The current URI for this page, for reference purposes)

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