{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"submitter":["Sawyer TK"],"funding":["NIDDK NIH HHS","NIGMS NIH HHS"],"pubmed_abstract":["Sphingolipid activator protein B (saposin B; SapB) is an essential activator of globotriaosylceramide (Gb3) catabolism by α-galactosidase A. However, the manner by which SapB stimulates α-galactosidase A activity remains unknown. To uncover the molecular mechanism of SapB presenting Gb3 to α-galactosidase A, we subjected the fluorescent substrate globotriaosylceramide-nitrobenzoxidazole (Gb3-NBD) to a series of biochemical and structural assays involving SapB. First, we showed that SapB stably binds Gb3-NBD using a fluorescence equilibrium binding assay, isolates Gb3-NBD from micelles, and facilitates α-galactosidase A cleavage of Gb3-NBD <i>in vitro</i>. Second, we crystallized SapB in the presence of Gb3-NBD and validated the ligand-bound assembly. Third, we captured transient interactio"],"journal":["bioRxiv : the preprint server for biology"],"pagination":["2024.04.04.584535"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11014568"],"repository":["biostudies-literature"],"pubmed_title":["Human Saposin B Ligand Binding and Presentation to α-Galactosidase A."],"pmcid":["PMC11014568"],"funding_grant_id":["P30 GM133894","R01 DK076877"],"pubmed_authors":["Garman SC","Staros JV","Bobst CE","Aral E","Sawyer TK"],"additional_accession":[]},"is_claimable":false,"name":"Human Saposin B Ligand Binding and Presentation to α-Galactosidase A.","description":"Sphingolipid activator protein B (saposin B; SapB) is an essential activator of globotriaosylceramide (Gb3) catabolism by α-galactosidase A. However, the manner by which SapB stimulates α-galactosidase A activity remains unknown. To uncover the molecular mechanism of SapB presenting Gb3 to α-galactosidase A, we subjected the fluorescent substrate globotriaosylceramide-nitrobenzoxidazole (Gb3-NBD) to a series of biochemical and structural assays involving SapB. First, we showed that SapB stably binds Gb3-NBD using a fluorescence equilibrium binding assay, isolates Gb3-NBD from micelles, and facilitates α-galactosidase A cleavage of Gb3-NBD <i>in vitro</i>. Second, we crystallized SapB in the presence of Gb3-NBD and validated the ligand-bound assembly. Third, we captured transient interactio","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Apr","modification":"2026-05-27T08:04:10.047Z","creation":"2026-05-27T03:07:56.564Z"},"accession":"S-EPMC11014568","cross_references":{"pubmed":["38617236"],"doi":["10.1101/2024.04.04.584535"]}}