4.8 Article

Multivalency, autoinhibition, and protein disorder in the regulation of interactions of dynein intermediate chain with dynactin and the nuclear distribution protein

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Summary: The N-terminal domain of dynein intermediate chain (N-IC) is a prototypical intrinsically disordered protein (IDP) that serves as a molecular scaffold for binding partners. Tertiary interactions in N-IC underlie differences in interactions with dynein partners p150(Glued) and NudE, showing that tertiary and secondary structures are coupled in IDPs. Interactions are attenuated when N-IC is bound to NudE, shifting the conformational ensemble to a more extended state with less structure.

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