Human keratin 1/10-1B tetramer structures reveal a knob-pocket mechanism in intermediate filament assembly.

ABSTRACT: To characterize keratin intermediate filament assembly mechanisms at atomic resolution, we determined the crystal structure of wild-type human keratin-1/keratin-10 helix 1B heterotetramer at 3.0 Å resolution. It revealed biochemical determinants for the A₁₁ mode of axial alignment in keratin filaments. Four regions on a hydrophobic face of the K1/K10-1B heterodimer dictated tetramer assembly: the N-terminal hydrophobic pocket (defined by L227^K1, Y230^K1, F231^K1, and F234^K1), the K10 hydrophobic stripe, K1 interaction residues, and the C-terminal anchoring knob (formed by F314^K1 and L318^K1). Mutation of both knob residues to alanine disrupted keratin 1B tetramer and full-length filament assembly. Individual knob res

SUBMITTER: Eldirany SA 

PROVIDER: S-EPMC6545558 | biostudies-literature | 2019 Jun

REPOSITORIES: biostudies-literature