Cell
Volume 30, Issue 1, August 1982, Pages 277-286
ArticleProteinchemical characterization of three structurally distinct domains along the protofilament unit of desmin 10 nm filaments
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Structural dynamics of the vimentin coiled-coil contact regions involved in filament assembly as revealed by hydrogen-deuterium exchange
2016, Journal of Biological ChemistryCitation Excerpt :The remaining segment of coil 2, here referred to as coil 2B, is in heptad configuration, allowing coiled-coil formation, including a “stutter” at position 350 that represents a brief interruption in the heptad pattern by a single hendecad repeat (16). A unique feature of vimentin and sequence-related IF proteins such as desmin and neurofilament proteins is represented by a short segment preceding coil 1A, the pre-coil domain (pcd), which exclusively contains amino acids that are compatible with α-helix formation, although no structure has been determined to date (orange box in Fig. 1A) (17). A corresponding structural motif is absent from other IF proteins such as keratins and nuclear lamins.
A different conformation for linker L12 in IF molecules in the molecular and filamentous forms: An hypothesis
2010, Journal of Structural BiologyNear-UV Circular Dichroism Reveals Structural Transitions of Vimentin Subunits during Intermediate Filament Assembly
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