A Disorder-to-Order Transition Activates an ATP-Independent Membrane Protein Chaperone
Journal of Molecular Biology(2020)
Abstract
•Substrate and activator drive cpSRP43 from an inactive, open state to an active, closed state.•The open state is characterized by disordered Ankyrin repeat motifs in the client binding domain.•Activator binding drives a disorder-to-order transition in the Ankyrin repeat domain.•The bridging helix mediates allosteric communication from ligand binding to the client binding domain.
MoreTranslated text
Key words
chaperone,membrane protein biogenesis,protein dynamics,ankyrin repeat proteins,NMR spectroscopy
AI Read Science
Must-Reading Tree
Example
![](https://originalfileserver.aminer.cn/sys/aminer/pubs/mrt_preview.jpeg)
Generate MRT to find the research sequence of this paper
Chat Paper
Summary is being generated by the instructions you defined