ArticleMoscow University biological sciences bulletin2021
Molecular Modeling of the HR2 and Transmembrane Domains of the SARS-CoV-2 S Protein in the Prefusion State.
Article in Moscow University biological sciences bulletin, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
SARS-CoV-2, the causative agent of COVID-19, remains the focus of research worldwide. SARS-CoV-2 entry into the cell starts with its S protein binding to the angiotensin-converting enzyme-2 (ACE2) expressed on the cell surface. The knowledge of the S protein's spatial structure is indispensable for understanding the molecular principles of its work. The S protein structure has been almost fully described using experimental approaches with the only exception for the protein's endodomain, the transmembrane domain, and the ectodomain parts adjacent to the latter. The paper reports molecular modelling of the S protein fragment corresponding to its coiled coil HR2 domain and fully palmitoylated transmembrane domain. Model stability in lipid bilayer was confirmed by all-atom and coarse-grained molecular dynamics simulations. It has been demonstrated that palmitoylation leads to a significant decrease in transmembrane domain mobility and local bilayer thickening, which may be relevant for protein trimerization.
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