A conserved histidine modulates HSPB5 structure to trigger chaperone activity in response to stress-related acidosis

A conserved histidine modulates HSPB5 structure to trigger chaperone activity in response to stress-related acidosis

Small heat shock proteins (sHSPs) are essential ‘holdase’ chaperones that form large assemblies and respond dynamically to pH and temperature stresses to protect client proteins from aggregation. While the alpha-crystallin domain (ACD) dimer of sHSPs is the universal building block, how the ACD tran...

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Bibliographic Details
Main Authors: Ponni Rajagopal, Eric Tse, Andrew J Borst, Scott P Delbecq, Lei Shi, Daniel R Southworth, Rachel E Klevit
Format: Article
Language:English
Published: eLife Sciences Publications Ltd 2015-05-01
Series:eLife
Subjects:
protein chaperone
heat shock protein
protein aggregation
electron microscopy
NMR
Online Access:https://elifesciences.org/articles/07304

Internet

https://elifesciences.org/articles/07304

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