Back to search

Article

How a pathogenic mutation impairs Hsp60 functional dynamics from monomeric to fully assembled states

2024-09-09

Abstract excerpt

Heat Shock Protein 60 kDa (Hsp60) is a mitochondrial chaperonin that cooperates with Hsp10 to drive the correct folding of client proteins. Monomers M of Hsp60 (featuring equatorial, intermediate, and apical domains) first assemble into 7-meric Single rings ( S ), then pairs of S interface equatorially to form 14-meric Double rings ( D ) that accommodate clients into their lumen. Recruitment of 7 Hsp10 molecul...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work
58d4c8f3-2fb8-5396-8981-3d6b0c399cb6
DOI
10.1101/2024.09.09.611948
Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest
Interactive article relationship graphSelect a related publication card to move it into the centre and load its closest explainable connections. Solid lines are source-backed structured connections. Dashed lines are semantic discovery signals and are not scientific evidence.
How a pathogenic mutation impairs Hsp60 functional dynamics from monomeric to fully assembled statesDOI 10.1101/2024.09.09.611948
Select a neighboring publication to make it the new centre.