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PubMed:15226294 JSONTXT 39 Projects

Annnotations TAB TSV DIC JSON TextAE Lectin_function IAV-Glycan

Id Subject Object Predicate Lexical cue
T1 0-57 Sentence denotes Sialic acid recognition by Vibrio cholerae neuraminidase.
T2 58-252 Sentence denotes Vibrio cholerae neuraminidase (VCNA) plays a significant role in the pathogenesis of cholera by removing sialic acid from higher order gangliosides to unmask GM1, the receptor for cholera toxin.
T3 253-490 Sentence denotes We previously showed that the structure of VCNA is composed of a central beta-propeller catalytic domain flanked by two lectin-like domains; however the nature of the carbohydrates recognized by these lectin domains has remained unknown.
T4 491-616 Sentence denotes We present here structures of the enzyme in complex with two substrates, alpha-2,3-sialyllactose and alpha-2,6-sialyllactose.
T5 617-783 Sentence denotes Both substrate complexes reveal the alpha-anomer of N-acetylneuraminic acid (Neu5Ac) bound to the N-terminal lectin domain, thereby revealing the role of this domain.
T6 784-953 Sentence denotes The large number of interactions suggest a relatively high binding affinity for sialic acid, which was confirmed by calorimetry, which gave a Kd approximately 30 microm.
T7 954-1143 Sentence denotes Saturation transfer difference NMR using a non-hydrolyzable substrate, Neu5,9Ac2-2-S-(alpha-2,6)-GlcNAcbeta1Me, was also used to map the ligand interactions at the VCNA lectin binding site.
T8 1144-1245 Sentence denotes It is well known that VCNA can hydrolyze both alpha-2,3- and alpha-2,6-linked sialic acid substrates.
T9 1246-1441 Sentence denotes In this study using alpha-2,3-sialyllactose co-crystallized with VCNA it was revealed that the inhibitor 2-deoxy-2,3-didehydro-N-acetylneuraminic acid (Neu5Ac2en) was bound at the catalytic site.
T10 1442-1569 Sentence denotes This observation supports the notion that VCNA can produce its own inhibitor and has been further confirmed by 1H NMR analysis.
T11 1570-1777 Sentence denotes The discovery of the sialic acid binding site in the N-lectin-like domain suggests that this might help target VCNA to sialic acid-rich environments, thereby enhancing the catalytic efficiency of the enzyme.