Fine mapping of hydrophobic contacts reassesses the organization of the first three dystrophin coiled-coil repeats.

ABSTRACT: Coiled-coil domain is a structural motif found in proteins crucial for achievement of central biological processes, such as cellular cohesion or neuro-transmission. The coiled-coil fold consists of alpha-helices bundle that can be repeated to form larger filament. Hydrophobic residues, distributed following a regular seven-residues' pattern, named heptad pattern, are commonly admitted to be essential for the formation and the stability of canonical coiled-coil repeats. Here we investigated the first three coiled-coil repeats (R1-R3) of the central domain of dystrophin, a scaffolding protein in muscle cells whose deficiency leads to Duchenne and Becker Muscular Dystrophies. By an atomic description of the hydrophobic interactions, we highlighted (i) that coiled-coil filament conformational

SUBMITTER: Mias-Lucquin D 

PROVIDER: S-EPMC6371207 | biostudies-literature | 2019 Mar

REPOSITORIES: biostudies-literature