{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Zhao Z"],"funding":["National Natural Science Foundation of China","Natural Science Foundation of Guangdong Province"],"pagination":["33421-33432"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7774290"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["5(51)"],"pubmed_abstract":["<i>Background</i>: Human urate transporter 1 (hURAT1) is the most pivotal therapeutic target for treating hyperuricemia. However, the molecular interactions between uric acid and URAT1 are still unknown due to lack of structural details. <i>Methods</i>: In the present study, several methods (homology modeling, sequence alignment, docking, and mutagenesis) were used to explain the atomistic mechanisms of uric acid transport of hURAT1. <i>Results</i>: Residues W357-F365 in the TMD7 and P484-R487 in the TMD11 present in the hURAT1 have unique roles in both binding to the uric acid and causing subsequent structural changes. These residues, located in the transport tunnel, were found to be related to the structural changes, as demonstrated by the reduced <i>V</i> <sub>max</sub> values and an un"],"journal":["ACS omega"],"pubmed_title":["Structural Insights into the Atomistic Mechanisms of Uric Acid Recognition and Translocation of Human Urate Anion Transporter 1."],"pmcid":["PMC7774290"],"funding_grant_id":["81773794","2018A0303130088","81974507"],"pubmed_authors":["Zhou P","Zhao Z","Li L","Nandakumar KS","Jiang Y","Li Y","Lin C","Lan Q","Cao Y","Tian Y","Chen Y","Pang J","Wu T"],"additional_accession":[]},"is_claimable":false,"name":"Structural Insights into the Atomistic Mechanisms of Uric Acid Recognition and Translocation of Human Urate Anion Transporter 1.","description":"<i>Background</i>: Human urate transporter 1 (hURAT1) is the most pivotal therapeutic target for treating hyperuricemia. However, the molecular interactions between uric acid and URAT1 are still unknown due to lack of structural details. <i>Methods</i>: In the present study, several methods (homology modeling, sequence alignment, docking, and mutagenesis) were used to explain the atomistic mechanisms of uric acid transport of hURAT1. <i>Results</i>: Residues W357-F365 in the TMD7 and P484-R487 in the TMD11 present in the hURAT1 have unique roles in both binding to the uric acid and causing subsequent structural changes. These residues, located in the transport tunnel, were found to be related to the structural changes, as demonstrated by the reduced <i>V</i> <sub>max</sub> values and an un","dates":{"release":"2020-01-01T00:00:00Z","publication":"2020 Dec","modification":"2026-04-29T17:54:57.431Z","creation":"2021-02-20T20:05:27Z"},"accession":"S-EPMC7774290","cross_references":{"pubmed":["33403304"],"doi":["10.1021/acsomega.0c05360"]}}