A structural vista of phosducin-like PhLP2A-chaperonin TRiC cooperation during the ATP-driven folding cycle.

Junsun Park Hyunmin KimDaniel GestautSeyeon LimAlexander LeitnerJudith Frydman Soung Hun Roh

Published in: bioRxiv : the preprint server for biology (2023)

Structural analysis of TRiC-mediated folding cycle with cochaperones PhLP2A and PFD.The interactions of PhLP2A and PFD with TRiC are mutually exclusive.PhLP2A domains interact in a subunit-specific manner with the TRiC chamber.PhLP2A domains are rearranged in ATP-closed TRiC to contact actin across the ring interface.

Keyphrases

single molecule
protein kinase