{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Zaigraev MM"],"funding":["Russian Science Foundation"],"pagination":["11"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9819746"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["24(1)"],"pubmed_abstract":["Ly6/uPAR proteins regulate many essential functions in the nervous and immune systems and epithelium. Most of these proteins contain single β-structural LU domains with three protruding loops and are glycosylphosphatidylinositol (GPI)-anchored to a membrane. The GPI-anchor role is currently poorly studied. Here, we investigated the positional and orientational preferences of six GPI-anchored proteins in the receptor-unbound state by molecular dynamics simulations. Regardless of the linker length between the LU domain and GPI-anchor, the proteins interacted with the membrane by polypeptide parts and N-/O-glycans. Lynx1, Lynx2, Lypd6B, and Ly6H contacted the membrane by the loop regions responsible for interactions with nicotinic acetylcholine receptors, while Lypd6 and CD59 demonstrated uni"],"journal":["International journal of molecular sciences"],"pubmed_title":["Orientational Preferences of GPI-Anchored Ly6/uPAR Proteins."],"pmcid":["PMC9819746"],"funding_grant_id":["19-74-20176"],"pubmed_authors":["Paramonov AS","Chugunov AO","Lyukmanova EN","Zaigraev MM","Shenkarev ZO"],"additional_accession":[]},"is_claimable":false,"name":"Orientational Preferences of GPI-Anchored Ly6/uPAR Proteins.","description":"Ly6/uPAR proteins regulate many essential functions in the nervous and immune systems and epithelium. Most of these proteins contain single β-structural LU domains with three protruding loops and are glycosylphosphatidylinositol (GPI)-anchored to a membrane. The GPI-anchor role is currently poorly studied. Here, we investigated the positional and orientational preferences of six GPI-anchored proteins in the receptor-unbound state by molecular dynamics simulations. Regardless of the linker length between the LU domain and GPI-anchor, the proteins interacted with the membrane by polypeptide parts and N-/O-glycans. Lynx1, Lynx2, Lypd6B, and Ly6H contacted the membrane by the loop regions responsible for interactions with nicotinic acetylcholine receptors, while Lypd6 and CD59 demonstrated uni","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Dec","modification":"2025-04-21T16:20:49.415Z","creation":"2025-04-21T16:20:49.415Z"},"accession":"S-EPMC9819746","cross_references":{"pubmed":["36613456"],"doi":["10.3390/ijms24010011"]}}