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. |