{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Yun JS"],"funding":["Hollings Cancer Center, Medical University of South Carolina","Ministry of Science ICT and Future Planning","NIBIB NIH HHS","National Institutes of Health","National Research Foundation of Korea","NIGMS NIH HHS"],"pagination":["89-95"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6145842"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["504(1)"],"pubmed_abstract":["The decapping exoribonuclease DXO functions in pre-mRNA capping quality control, and shows multiple biochemical activities such as decapping, deNADding, pyrophosphohydrolase, and 5'-3' exoribonuclease activities. Previous studies revealed the molecular mechanisms of DXO based on the structures in complexes with a product, substrate mimic, cap analogue, and 3'-NADP<sup>+</sup>. Despite several reports on the substrate-specific reaction mechanism, the inhibitory mechanism of DXO remains elusive. Here, we demonstrate that adenosine 3', 5'-bisphosphate (pAp), a known inhibitor of the 5'-3' exoribonuclease Xrn1, inhibits the nuclease activity of DXO based on the results of structural and biochemical experiments. We determined the crystal structure of the DXO-pAp-Mg<sup>2+</sup> complex at 1.8 Å"],"journal":["Biochemical and biophysical research communications"],"pubmed_title":["Molecular mechanism for the inhibition of DXO by adenosine 3',5'-bisphosphate."],"pmcid":["PMC6145842"],"funding_grant_id":["2016R1C1B2009691","R35 GM118093","GM118093","P30 EB009998","2013R1A1A1061391"],"pubmed_authors":["Kim S","Chang JH","Yun JS","Tong L","Choi YJ","Yoon JH","Son YJ"],"additional_accession":[]},"is_claimable":false,"name":"Molecular mechanism for the inhibition of DXO by adenosine 3',5'-bisphosphate.","description":"The decapping exoribonuclease DXO functions in pre-mRNA capping quality control, and shows multiple biochemical activities such as decapping, deNADding, pyrophosphohydrolase, and 5'-3' exoribonuclease activities. Previous studies revealed the molecular mechanisms of DXO based on the structures in complexes with a product, substrate mimic, cap analogue, and 3'-NADP<sup>+</sup>. Despite several reports on the substrate-specific reaction mechanism, the inhibitory mechanism of DXO remains elusive. Here, we demonstrate that adenosine 3', 5'-bisphosphate (pAp), a known inhibitor of the 5'-3' exoribonuclease Xrn1, inhibits the nuclease activity of DXO based on the results of structural and biochemical experiments. We determined the crystal structure of the DXO-pAp-Mg<sup>2+</sup> complex at 1.8 Å","dates":{"release":"2018-01-01T00:00:00Z","publication":"2018 Sep","modification":"2025-06-01T03:31:42.967Z","creation":"2019-10-11T07:16:16Z"},"accession":"S-EPMC6145842","cross_references":{"pubmed":["30180947"],"doi":["10.1016/j.bbrc.2018.08.135"]}}