Desmin-binding specificities of two desmin CNBr fragments that correspond to the headpiece domain and Helix 1B.
D88 and D109, two cyanogen bromide fragments of desmin which essentially correspond to the amino terminal headpiece domain and Helix 1B, respectively, bind to intact desmin with different topological specificities. D88, the headpiece domain fragment, binds only to the headpiece of intact desmin. In contrast, D109, which encompasses Helix 1B and most of the linker L10 binds to desmin even when its headpiece is removed. Additionally, these fragments only bind desmin if they are present during filament assembly; they do not bind pre-assembled desmin IF or tetramers. These observations suggest that, while alpha-helical coiled-coil interaction between rod domains provides the major driving force behind IF protein dimer formation, homophilic binding of head domains of these proteins may provide an additional stabilizing force and/or specify axial registration in certain IF proteins.
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Department of Anatomy and Cell Biology, University of Cincinnati College of Medicine, Ohio 45267-0521.
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D000818:Animals; D002645:Chickens; D003893:Desmin / Q000378:metabolism*; D007382:Intermediate Filaments / Q000378:metabolism; D010446:Peptide Fragments / Q000378:metabolism*; D011485:Protein Binding / Q000187:drug effects; D011487:Protein Conformation
D003893:Desmin; D010446:Peptide Fragments