Ontology highlight
ABSTRACT:
SUBMITTER: Finci LI
PROVIDER: S-EPMC10908828 | biostudies-literature | 2024 Mar
REPOSITORIES: biostudies-literature
Finci Lorenzo I LI Chakrabarti Mayukh M Gulten Gulcin G Finney Joseph J Grose Carissa C Fox Tara T Yang Renbin R Nissley Dwight V DV McCormick Frank F Esposito Dominic D Balius Trent E TE Simanshu Dhirendra K DK
Communications biology 20240302 1
RAF kinases are integral to the RAS-MAPK signaling pathway, and proper RAF1 folding relies on its interaction with the chaperone HSP90 and the cochaperone CDC37. Understanding the intricate molecular interactions governing RAF1 folding is crucial for comprehending this process. Here, we present a cryo-EM structure of the closed-state RAF1-HSP90-CDC37 complex, where the C-lobe of the RAF1 kinase domain binds to one side of the HSP90 dimer, and an unfolded N-lobe segment of the RAF1 kinase domain ...[more]