Molecular modeling of vimentin filament assembly

Proteins
D T Downing

Abstract

Intermediate-filament forming proteins are known to form rod-shaped dimers that are calculated to be 45 nm in length. Molecular modeling indicates that the dimerization is promoted by interchain hydrophobic interactions between sections of alpha helix and beta helix. Further aggregation involves the formation of tetramers in which two dimers are anti-parallel and staggered to two characteristic degrees of overlap. Modeling indicated that the degrees of stagger are dictated by the association of sections of alpha helix in 4-chain bundles, in which hydrophobic side chains are sequestered from contact with water. The staggered arrangement of two dimers produces a tetramer having sections of 2-chain rod in which hydrophobic side chains are exposed to water. Extension of the tetramer to form protofilaments may be driven by associations with the 2-chain regions that reduce aqueous exposure of the hydrophobic side chains. Exposure of hydrophobic groups may be reduced by the 2-chain regions folding back upon themselves so that the entire tetramer becomes a 4-chain conformation. This prediction is in line with electron microscope data showing that mixtures of the lower oligomers contain rods of uniform thickness ranging upwards from 45 ...Continue Reading

References

Nov 20, 1986·Journal of Molecular Biology·R A QuinlanJ Engel
Jan 1, 1988·Annual Review of Biochemistry·P M Steinert, D R Roop
Jun 1, 1988·Proceedings of the National Academy of Sciences of the United States of America·K C ChouH A Scheraga
Nov 1, 1986·Molecular and Cellular Biology·S FerrariR Baserga
Jun 1, 1993·The Journal of Investigative Dermatology·P M Steinert

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Citations

Jul 17, 1999·The Journal of Peptide Research : Official Journal of the American Peptide Society·N D Lazo, D T Downing
Jun 27, 1997·Biochemical and Biophysical Research Communications·N D Lazo, D T Downing
Jun 19, 1998·Current Opinion in Structural Biology·H Herrmann, U Aebi

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