ArticleJournal of molecular modeling2016
Investigating the substrate binding mechanism of sulfotransferase 2A1 based on substrate tunnel analysis: a molecular dynamics simulation study.
Article in Journal of molecular modeling, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
1 citing paper in PubMed.
- From Steroid and Drug Metabolism to Glycobiology, Using Sulfotransferase Structures to Understand and Tailor Function.Drug metabolism and disposition: the biological fate of chemicals · 2022Review
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Authors and funding
7 authors.
Funding
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Abstract
Cytosolic sulfotransferases (SULTs) catalyze the transfer of a sulfonate group from the unique cofactor 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to a large number of diverse substrates. In this work, tunnels that facilitate the transport of substrates in the enzyme were studied, with and without bound cofactor, using extensive molecular dynamics simulations. Residues making up tunnels, as well as residues forming bottlenecks to the tunnels, were identified. Conformation analysis of the active-site cap was also performed. We found that binding of cofactor could significantly narrow the tunnel based on the closing of the active-site cap to the enzyme. The roles of the key residues identified in this work deserve further exploration experimentally.
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Registered trials
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