{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Wang T"],"funding":["National Institutes of Health","NIGMS NIH HHS","NIH HHS"],"pagination":["20305-20312"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5724015"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["292(49)"],"pubmed_abstract":["Non-steroidal anti-inflammatory drugs (NSAIDs) are among the most commonly prescribed drugs worldwide-more than 111 million prescriptions were written in the United States in 2014. NSAIDs allosterically inhibit cytosolic sulfotransferases (SULTs) with high specificity and therapeutically relevant affinities. This study focuses on the interactions of SULT1A1 and mefenamic acid (MEF)-a potent, highly specific NSAID inhibitor of 1A1. Here, the first structure of an NSAID allosteric site-the MEF-binding site of SULT1A1-is determined using spin-label triangulation NMR. The structure is confirmed by site-directed mutagenesis and provides a molecular framework for understanding NSAID binding and isoform specificity. The mechanism of NSAID inhibition is explored using molecular dynamics and equili"],"journal":["The Journal of biological chemistry"],"pubmed_title":["The NSAID allosteric site of human cytosolic sulfotransferases."],"pmcid":["PMC5724015"],"funding_grant_id":["R01 GM106158","GM121849","S10 OD016305","GM106158","R01 GM121849"],"pubmed_authors":["Cook I","Wang T","Leyh TS"],"additional_accession":[]},"is_claimable":false,"name":"The NSAID allosteric site of human cytosolic sulfotransferases.","description":"Non-steroidal anti-inflammatory drugs (NSAIDs) are among the most commonly prescribed drugs worldwide-more than 111 million prescriptions were written in the United States in 2014. NSAIDs allosterically inhibit cytosolic sulfotransferases (SULTs) with high specificity and therapeutically relevant affinities. This study focuses on the interactions of SULT1A1 and mefenamic acid (MEF)-a potent, highly specific NSAID inhibitor of 1A1. Here, the first structure of an NSAID allosteric site-the MEF-binding site of SULT1A1-is determined using spin-label triangulation NMR. The structure is confirmed by site-directed mutagenesis and provides a molecular framework for understanding NSAID binding and isoform specificity. The mechanism of NSAID inhibition is explored using molecular dynamics and equili","dates":{"release":"2017-01-01T00:00:00Z","publication":"2017 Dec","modification":"2026-05-03T03:51:43.767Z","creation":"2019-03-27T00:10:56Z"},"accession":"S-EPMC5724015","cross_references":{"pubmed":["29038294"],"doi":["10.1074/jbc.m117.817387","10.1074/jbc.M117.817387"]}}