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Project

Structural basis for disease-causing mutations in the molecular chaperone HSP27.

Small heat-shock proteins (sHSPs) are ubiquitously expressed molecular chaperones that play vital roles in the maintenance of protein homeostasis. Our structural understanding of these chaperones, however, remains limited because sHSPs assemble into large, heterogeneous oligomers that have proven refractory to traditional structural biology approaches. So far, most work has relied on heavily engineered variants to isolate a single oligomeric form, which may no longer represent a biologically meaningful state. Our recent work showed that this roadblock can be circumvented by studying disease-causing variants that interfere with central properties of these chaperones. Here, we propose to study the structural consequences of HSP27 in which mutations cause motor neuropathies.
Date:1 Apr 2021 →  31 Mar 2022
Keywords:EXPERIMENTAL STUDY, MOLECULAR DYNAMICS
Disciplines:Molecular biophysics, Neurological and neuromuscular diseases