<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>286(22)</volume><submitter>Sato Y</submitter><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</pubmed_abstract><journal>The Journal of biological chemistry</journal><pagination>19446-58</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC3103324</full_dataset_link><repository>biostudies-literature</repository><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.</pubmed_title><pmcid>PMC3103324</pmcid><pubmed_authors>Okuyama S</pubmed_authors><pubmed_authors>Yamamoto N</pubmed_authors><pubmed_authors>Hori K</pubmed_authors><pubmed_authors>Hirayama M</pubmed_authors><pubmed_authors>Morimoto K</pubmed_authors><pubmed_authors>Sato Y</pubmed_authors></additional><is_claimable>false</is_claimable><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.</name><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</description><dates><release>2011-01-01T00:00:00Z</release><publication>2011 Jun</publication><modification>2026-05-03T07:35:00.684Z</modification><creation>2019-03-27T00:42:04Z</creation></dates><accession>S-EPMC3103324</accession><cross_references><pubmed>21460211</pubmed><doi>10.1074/jbc.M110.216655</doi><doi>10.1074/jbc.m110.216655</doi></cross_references></HashMap>