{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Giladi M"],"funding":["Israel Cancer Research Fund (Israel Cancer Research Fund, Inc.)","Israel Science Foundation","Israel Science Foundation (ISF)","Israel Cancer Research Fund"],"pagination":["10786"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12663261"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["16(1)"],"pubmed_abstract":["Human cis-prenyltransferase (hcis-PT) synthesizes long-chain isoprenoids essential for N-linked protein glycosylation. This heteromeric complex comprises the catalytic subunit DHDDS and the regulatory Nogo-B receptor (NgBR). Although NgBR dramatically enhances DHDDS activity, the molecular basis for this allosteric regulation remains unclear. Here, we combined crystallography, hydrogen-deuterium exchange mass spectrometry (HDX-MS), molecular dynamics simulations, and network analysis to uncover the structural dynamics and communication pathways within hcis-PT. By solving the apo structure of hcis-PT, we reveal only a localized flexibility at the active site and the NgBR C-terminus. However, HDX-MS demonstrated widespread substrate-induced stabilization, particularly at the NgBR βD-βE loop,"],"journal":["Nature communications"],"pubmed_title":["Structural mechanisms of allosteric regulation in the human cis-prenyltransferase complex."],"pmcid":["PMC12663261"],"funding_grant_id":["2337/25","1289067"],"pubmed_authors":["Man P","Guardiani C","Haitin Y","Vankova P","Giacomello A","Giladi M","Aviram L","Kredi S","Gaizinger Y"],"additional_accession":[]},"is_claimable":false,"name":"Structural mechanisms of allosteric regulation in the human cis-prenyltransferase complex.","description":"Human cis-prenyltransferase (hcis-PT) synthesizes long-chain isoprenoids essential for N-linked protein glycosylation. This heteromeric complex comprises the catalytic subunit DHDDS and the regulatory Nogo-B receptor (NgBR). Although NgBR dramatically enhances DHDDS activity, the molecular basis for this allosteric regulation remains unclear. Here, we combined crystallography, hydrogen-deuterium exchange mass spectrometry (HDX-MS), molecular dynamics simulations, and network analysis to uncover the structural dynamics and communication pathways within hcis-PT. By solving the apo structure of hcis-PT, we reveal only a localized flexibility at the active site and the NgBR C-terminus. However, HDX-MS demonstrated widespread substrate-induced stabilization, particularly at the NgBR βD-βE loop,","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Nov","modification":"2026-07-15T07:47:49.562Z","creation":"2026-07-01T03:08:12.75Z"},"accession":"S-EPMC12663261","cross_references":{"pubmed":["41315348"],"doi":["10.1038/s41467-025-65833-6"]}}