{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Boren DM"],"funding":["Israel Science Foundation","Israel Cancer Association","National Institutes of Health","NIH HHS","NIGMS NIH HHS","National Science Foundation","Israel Cancer Research Fund"],"pagination":["e70167"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12102762"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["34(6)"],"pubmed_abstract":["Prenyl chains come in multiple sizes, fulfilling unique and essential functions across all domains of life. Prenyl chains are synthesized by prenyltransferase proteins. Despite their structural similarity, prenyltransferases exhibit substantial functional diversity to create lipophilic products of varying lengths. Human cis-prenyltransferase (h-cisPT) is a tetrameric enzyme responsible for the synthesis of long prenyl chains, consisting of 20-prenyl-unit products that are essential to specific posttranslational modifications such as N-glycosylation upon downstream processing. These long products are hypothesized to transfer from h-cisPT to the ER membrane, but the mechanism of this transfer is not known. We use molecular dynamics simulations to identify a consistent membrane binding pose f"],"journal":["Protein science : a publication of the Protein Society"],"pubmed_title":["Identifying and quantifying membrane interactions of the protein human cis-prenyltransferase."],"pmcid":["PMC12102762"],"funding_grant_id":["R35GM155317","19202","1653/21","R35 GM155317","20230029","24115","1721/16","NSF 1828149"],"pubmed_authors":["Boren DM","Haitin Y","Vermaas JV","Giladi M","Kredi S","Positselskaya E"],"additional_accession":[]},"is_claimable":false,"name":"Identifying and quantifying membrane interactions of the protein human cis-prenyltransferase.","description":"Prenyl chains come in multiple sizes, fulfilling unique and essential functions across all domains of life. Prenyl chains are synthesized by prenyltransferase proteins. Despite their structural similarity, prenyltransferases exhibit substantial functional diversity to create lipophilic products of varying lengths. Human cis-prenyltransferase (h-cisPT) is a tetrameric enzyme responsible for the synthesis of long prenyl chains, consisting of 20-prenyl-unit products that are essential to specific posttranslational modifications such as N-glycosylation upon downstream processing. These long products are hypothesized to transfer from h-cisPT to the ER membrane, but the mechanism of this transfer is not known. We use molecular dynamics simulations to identify a consistent membrane binding pose f","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Jun","modification":"2026-06-01T15:33:32.768Z","creation":"2026-04-08T13:38:00.391Z"},"accession":"S-EPMC12102762","cross_references":{"pubmed":["40411431"],"doi":["10.1002/pro.70167"]}}