Cell
Volume 30, Issue 1, August 1982, Pages 277-286
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Article
Proteinchemical characterization of three structurally distinct domains along the protofilament unit of desmin 10 nm filaments

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Abstract

Limited chymotryptic cleavage of soluble chicken gizzard desmin protofilaments allows the characterization of three structurally distinct domains. A surface-exposed very basic amino-terminal region (the headpiece) with an amino acid sequence excluding a-helical organization (7.5 kd) is separated from the perhaps globular carboxy-terminal 48 residues (the tailpiece) by a distinctly different middle domain of approximately 330 residues. This 38 kd domain is very rich in α-helix (at least 83%), and electron microscopy reveals a thin rod with a length of 500 ± 50 Å. Amino acid sequence data also show that the rod domain is interrupted by a nonhelical portion. An a-helical array is able to form a coiled-coil spanning the carboxy-terminal half of the 38 kd domain. The a-type diffraction pattern of 10 nm filaments arises from a coiled-coil conformation displayed through most but not all of the middle domain of the protofilaments.

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Cited by (173)

  • Structural dynamics of the vimentin coiled-coil contact regions involved in filament assembly as revealed by hydrogen-deuterium exchange

    2016, Journal of Biological Chemistry
    Citation 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.

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