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PubMed:26253171 JSONTXT

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GlyCosmos6-UBERON

Id Subject Object Predicate Lexical cue
T1 1012-1017 Body_part denotes helix
T2 1062-1067 Body_part denotes helix

sentences

Id Subject Object Predicate Lexical cue
T1 0-161 Sentence denotes Interactions of Yeast Dynein with Dynein Light Chain and Dynactin: GENERAL IMPLICATIONS FOR INTRINSICALLY DISORDERED DUPLEX SCAFFOLDS IN MULTIPROTEIN ASSEMBLIES.
T2 162-333 Sentence denotes Intrinsically disordered protein (IDP) duplexes composed of two IDP chains cross-linked by bivalent partner proteins form scaffolds for assembly of multiprotein complexes.
T3 334-557 Sentence denotes The N-terminal domain of dynein intermediate chain (N-IC) is one such IDP that forms a bivalent scaffold with multiple dynein light chains including LC8, a hub protein that promotes duplex formation of diverse IDP partners.
T4 558-618 Sentence denotes N-IC also binds a subunit of the dynein regulator, dynactin.
T5 619-787 Sentence denotes Here we characterize interactions of a yeast ortholog of N-IC (N-Pac11) with yeast LC8 (Dyn2) or with the intermediate chain-binding subunit of yeast dynactin (Nip100).
T6 788-943 Sentence denotes Residue level changes in Pac11 structure are monitored by NMR spectroscopy, and binding energetics are monitored by isothermal titration calorimetry (ITC).
T7 944-1116 Sentence denotes N-Pac11 is monomeric and primarily disordered except for a single α-helix (SAH) at the N terminus and a short nascent helix, LH, flanked by the two Dyn2 recognition motifs.
T8 1117-1258 Sentence denotes Upon binding Dyn2, the only Pac11 residues making direct protein-protein interactions are in and immediately flanking the recognition motifs.
T9 1259-1305 Sentence denotes Dyn2 binding also orders LH residues of Pac11.
T10 1306-1495 Sentence denotes Upon binding Nip100, only Pac11 SAH residues make direct protein-protein interactions, but LH residues at a distant sequence position and L1 residues in an adjacent linker are also ordered.
T11 1496-1621 Sentence denotes The long distance, ligand-dependent ordering of residues reveals new elements of dynamic structure within IDP linker regions.