Conformational Flexibility of p150^Glued(1-191) Subunit of Dynactin Assembled with Microtubules.

ABSTRACT: Microtubule (MT)-associated proteins perform diverse functions in cells. These functions are dependent on their interactions with MTs. Dynactin, a cofactor of dynein motor, assists the binding of dynein to various organelles and is crucial to the long-distance processivity of dynein-based complexes. The largest subunit of dynactin, the p150^Glued, contains an N-terminus segment that is responsible for the MT-binding interactions and long-range processivity of dynactin. We employed solution and magic angle spinning NMR spectroscopy to characterize the structure and dynamics of the p150^Glued N-terminal region, both free and in complex with polymerized MTs. This 191-residue region encompasses the cytoskeleton-associated protein glycine-rich domain, the basic domain, and s

SUBMITTER: Guo C 

PROVIDER: S-EPMC6731383 | biostudies-literature | 2019 Sep

REPOSITORIES: biostudies-literature