{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Pan B"],"funding":["National Institute of Neurological Disorders and Stroke","University of Pennsylvania","Heiwa Nakajima Foundation","NINDS NIH HHS","National Institute of General Medical Sciences","NIGMS NIH HHS","NIH HHS","Shizuoka University"],"pagination":["14019-14030"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10728591"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["145(25)"],"pubmed_abstract":["N-terminal acetylation is a chemical modification carried out by N-terminal acetyltransferases. A major member of this enzyme family, NatB, acts on much of the human proteome, including α-synuclein (αS), a synaptic protein that mediates vesicle trafficking. NatB acetylation of αS modulates its lipid vesicle binding properties and amyloid fibril formation, which underlies its role in the pathogenesis of Parkinson's disease. Although the molecular details of the interaction between human NatB (hNatB) and the N-terminus of αS have been resolved, whether the remainder of the protein plays a role in interacting with the enzyme is unknown. Here, we execute the first synthesis, by native chemical ligation, of a bisubstrate inhibitor of NatB consisting of coenzyme A and full-length human αS, addit"],"journal":["Journal of the American Chemical Society"],"pubmed_title":["Semi-Synthetic CoA-α-Synuclein Constructs Trap N-Terminal Acetyltransferase NatB for Binding Mechanism Studies."],"pmcid":["PMC10728591"],"funding_grant_id":["RF1 NS125770","S10 OD030460","T32 GM133398","R01 NS120625","NS125770","R35 GM118090","R01 NS103873","R35 GM1118090","T32 GM132039"],"pubmed_authors":["Gardner SM","Deng S","Shimogawa M","Petersson EJ","Pan B","Perez RM","Schultz K","Sato K","Rhoades E","Marmorstein R"],"additional_accession":[]},"is_claimable":false,"name":"Semi-Synthetic CoA-α-Synuclein Constructs Trap N-Terminal Acetyltransferase NatB for Binding Mechanism Studies.","description":"N-terminal acetylation is a chemical modification carried out by N-terminal acetyltransferases. A major member of this enzyme family, NatB, acts on much of the human proteome, including α-synuclein (αS), a synaptic protein that mediates vesicle trafficking. NatB acetylation of αS modulates its lipid vesicle binding properties and amyloid fibril formation, which underlies its role in the pathogenesis of Parkinson's disease. Although the molecular details of the interaction between human NatB (hNatB) and the N-terminus of αS have been resolved, whether the remainder of the protein plays a role in interacting with the enzyme is unknown. Here, we execute the first synthesis, by native chemical ligation, of a bisubstrate inhibitor of NatB consisting of coenzyme A and full-length human αS, addit","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Jun","modification":"2025-04-21T15:58:17.109Z","creation":"2025-04-21T15:58:17.109Z"},"accession":"S-EPMC10728591","cross_references":{"pubmed":["37319422"],"doi":["10.1021/jacs.3c03887"]}}