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PubMed:17897951 JSONTXT 27 Projects

Annnotations TAB TSV DIC JSON TextAE Lectin_function IAV-Glycan

Id Subject Object Predicate Lexical cue
T1 0-112 Sentence denotes Structural basis for innate immune sensing by M-ficolin and its control by a pH-dependent conformational switch.
T2 113-261 Sentence denotes Ficolins are soluble oligomeric proteins with lectin-like activity, assembled from collagen fibers prolonged by fibrinogen-like recognition domains.
T3 262-459 Sentence denotes They act as innate immune sensors by recognizing conserved molecular markers exposed on microbial surfaces and thereby triggering effector mechanisms such as enhanced phagocytosis and inflammation.
T4 460-601 Sentence denotes In humans, L- and H-ficolins have been characterized in plasma, whereas a third species, M-ficolin, is secreted by monocytes and macrophages.
T5 602-913 Sentence denotes To decipher the molecular mechanisms underlying their recognition properties, we previously solved the structures of the recognition domains of L- and H-ficolins, in complex with various model ligands (Garlatti, V., Belloy, N., Martin, L., Lacroix, M., Matsushita, M., Endo, Y., Fujita, T., Fontecilla-Camps, J.
T6 914-928 Sentence denotes C., Arlaud, G.
T7 929-945 Sentence denotes J., Thielens, N.
T8 946-982 Sentence denotes M., and Gaboriaud, C. (2007) EMBO J.
T9 983-996 Sentence denotes 24, 623-633).
T10 997-1204 Sentence denotes We now report the ligand-bound crystal structures of the recognition domain of M-ficolin, determined at high resolution (1.75-1.8 A), which provides the first structural insights into its binding properties.
T11 1205-1303 Sentence denotes Interaction with acetylated carbohydrates differs from the one previously described for L-ficolin.
T12 1304-1471 Sentence denotes This study also reveals the structural determinants for binding to sialylated compounds, a property restricted to human M-ficolin and its mouse counterpart, ficolin B.
T13 1472-1662 Sentence denotes Finally, comparison between the ligand-bound structures obtained at neutral pH and nonbinding conformations observed at pH 5.6 reveals how the ligand binding site is dislocated at acidic pH.
T14 1663-1764 Sentence denotes This means that the binding function of M-ficolin is subject to a pH-sensitive conformational switch.
T15 1765-1868 Sentence denotes Considering that the homologous ficolin B is found in the lysosomes of activated macrophages (Runza, V.
T16 1869-1932 Sentence denotes L., Hehlgans, T., Echtenacher, B., Zahringer, U., Schwaeble, W.
T17 1933-1951 Sentence denotes J., and Mannel, D.
T18 1952-1964 Sentence denotes N. (2006) J.
T19 1965-1979 Sentence denotes Endotoxin Res.
T20 1980-2082 Sentence denotes 12, 120-126), we propose that this switch could play a physiological role in such acidic compartments.