{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["286(22)"],"submitter":["Sato Y"],"pubmed_abstract":["The complete amino acid sequence of a lectin from the green alga Boodlea coacta (BCA), which was determined by a combination of Edman degradation of its peptide fragments and cDNA cloning, revealed the following: 1) B. coacta used a noncanonical genetic code (where TAA and TAG codons encode glutamine rather than a translation termination), and 2) BCA consisted of three internal tandem-repeated domains, each of which contains the sequence motif similar to the carbohydrate-binding site of Galanthus nivalis agglutinin-related lectins. Carbohydrate binding specificity of BCA was examined by a centrifugal ultrafiltration-HPLC assay using 42 pyridylaminated oligosaccharides. BCA bound to high mannose-type N-glycans but not to the complex-type, hybrid-type core structure of N-glycans or oligosacc"],"journal":["The Journal of biological chemistry"],"pagination":["19446-58"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3103324"],"repository":["biostudies-literature"],"pubmed_title":["High mannose-binding lectin with preference for the cluster of alpha1-2-mannose from the green alga Boodlea coacta is a potent entry inhibitor of HIV-1 and influenza viruses."],"pmcid":["PMC3103324"],"pubmed_authors":["Okuyama S","Yamamoto N","Hori K","Hirayama M","Morimoto K","Sato Y"],"additional_accession":[]},"is_claimable":false,"name":"High mannose-binding lectin with preference for the cluster of alpha1-2-mannose from the green alga Boodlea coacta is a potent entry inhibitor of HIV-1 and influenza viruses.","description":"The complete amino acid sequence of a lectin from the green alga Boodlea coacta (BCA), which was determined by a combination of Edman degradation of its peptide fragments and cDNA cloning, revealed the following: 1) B. coacta used a noncanonical genetic code (where TAA and TAG codons encode glutamine rather than a translation termination), and 2) BCA consisted of three internal tandem-repeated domains, each of which contains the sequence motif similar to the carbohydrate-binding site of Galanthus nivalis agglutinin-related lectins. Carbohydrate binding specificity of BCA was examined by a centrifugal ultrafiltration-HPLC assay using 42 pyridylaminated oligosaccharides. BCA bound to high mannose-type N-glycans but not to the complex-type, hybrid-type core structure of N-glycans or oligosacc","dates":{"release":"2011-01-01T00:00:00Z","publication":"2011 Jun","modification":"2026-05-03T07:35:00.684Z","creation":"2019-03-27T00:42:04Z"},"accession":"S-EPMC3103324","cross_references":{"pubmed":["21460211"],"doi":["10.1074/jbc.M110.216655","10.1074/jbc.m110.216655"]}}