Article
The p.K90N mutation in human HSPB5 highlights the critical role of lysine 90 in chaperone function and structural integrity.
Archives of biochemistry and biophysics - 1 Jul 2025
Ghaffari Ahmad Reza, Mirzaei Zahra, Shahsavani Mohammad Bagher, Somee Leila Rezaei, Stroylova Yulia Y, Barinova Ksenia V, Amanlou Massoud, Muronetz Vladimir I, Habibi-Rezaei Mehran, Saboury Ali Akbar, Moosavi-Movahedi Ali Akbar, Yousefi Reza
Abstract excerpt
HSPB5 (αB-crystallin), a small heat shock protein, stabilizes proteins and prevents misfolded protein aggregation through dynamic oligomer formation. Mutations in HSPB5 can result in diseases such as myopathy and cataracts. This study focuses on the myopathy-associated p.K90N mutation in the α-crystallin domain and its impact on the structure and function of human HSPB5. The recombinant mutated protein was...
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