Structural and functional analysis of actin point mutations leading to nemaline myopathy to elucidate their role in actin function.

ABSTRACT: In this work, we analyzed 78 mutations in the actin protein that cause the disease nemaline myopathy. We analyzed how these mutations are distributed in important regions of the actin molecule (folding nucleus, core of the filament, amyloidogenic regions, disordered regions, regions involved in interaction with other proteins). It was found that 54 mutations (43 residues) fall into the folding nucleus (Ф ≥ 0.5), 11 mutations (10 residues) into the filament core, 14 mutations into the amyloidogenic regions (11 residues), 14 mutations (9 residues) in the unstructured regions, and 24 mutations (22 residues) in regions involved in interaction with other proteins. It was also found that the occurrence of single mutations G44V, V45F, T68I, P72R, K338I and S350L leads to the appearance of

SUBMITTER: Glyakina AV 

PROVIDER: S-EPMC9842827 | biostudies-literature | 2022 Dec

REPOSITORIES: biostudies-literature