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

EMBO J. 2019-04; 
Eldirany SA, Ho M, Hinbest AJ, Lomakin IB, Bunick CG.
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Gene Synthesis ...pET-based plasmids of K1-1B (res. 226–331), K10-1B (res. 195–296), K1S233L-1B (res. 226–331), and the K1-1B mutants F314A, L318A, and F314A+L318A were purchased from GenScript (Piscataway, NJ). pET-21a(+)-based plasmids of human full-length wild-type K1, K1 containing F314A + L318A mutations, wild-type K8, K8 containing F223A + L227A mutations, wild-type vimentin, and vimentin containing F233A + L237A mutations were purchased from GenScript (Piscataway, NJ)... Get A Quote
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摘要

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 L227K1, Y230K1, F231K1, and F234K1), the K10 hydrophobic stripe, K1 interaction residues, and the C-terminal anchoring knob (formed by F314K1 and L318K1). Mutation of both knob residues to alanine disrupted keratin 1B tetramer and full-length filament assembly. Individual knob... More

关键词

intermediate filament; keratin; skin disease; structure; vimentin