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Related Experiment Videos

Structural features of keratin intermediate filaments

P M Steinert1, A C North, D A Parry

  • 1Skin Biology Branch, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, Maryland 20892-2755.

The Journal of Investigative Dermatology
|November 1, 1994
PubMed
Summary

Researchers modeled keratin intermediate filament (KIF) structure, revealing insights into coiled-coil rope formation and molecular packing. This study refines understanding of KIF assembly and potential links to genodermatoses.

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Area of Science:

  • Biophysics
  • Structural Biology
  • Molecular Cell Biology

Background:

  • Keratin intermediate filaments (KIFs) are crucial structural components in epithelial cells.
  • KIF assembly begins with type I/type II heterodimer formation, creating a coiled-coil rope structure.
  • The precise molecular arrangement and packing within KIFs remain incompletely understood.

Purpose of the Study:

  • To model structural irregularities within the keratin coiled-coil rope, specifically the L2 link and a heptad discontinuity.
  • To investigate the molecular packing and alignment of neighboring KIF molecules.
  • To provide new constraints for models of KIF structure and assembly.

Main Methods:

  • Computational modeling of the L2 link and heptad discontinuity in segment 2B of the coiled-coil rope.

Related Experiment Videos

  • Analysis of crosslinking experimental data to determine KIF molecular alignment and overlap.
  • Comparison of predicted axial periodicity with electron microscopy data.

    • Main Results:

    • The L2 link involves a ~180-degree turn in coiled-coil orientation over eight residues.
    • A heptad discontinuity in segment 2B causes minimal distortion to the coiled-coil rope.
    • Crosslinking data suggest anti-parallel alignment of neighboring KIF molecules with ~1 nm overlap, predicting a 22.6 nm axial periodicity observed via electron microscopy.
    • Mutations in keratin genes causing genodermatoses are concentrated in the molecular overlap region.

    Conclusions:

    • The study provides refined models for structural elements within the keratin coiled-coil rope.
    • Molecular packing involves anti-parallel alignment and significant overlap, potentially forming protofibrils.
    • These findings offer new constraints for understanding KIF assembly and the structural basis of genodermatoses.