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Matches in SemOpenAlex for { <https://semopenalex.org/work/W1995278329> ?p ?o ?g. }

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• W1995278329 startingPage "46" @default.
• W1995278329 abstract "Cytoskeletal intermediate filaments (IFs) assemble from the elementary dimers based on a segmented α-helical coiled-coil (CC) structure. Crystallographic studies of IF protein fragments remain the main route to access their atomic structure. To enable crystallization, such fragments must be sufficiently short. As a consequence, they often fail to assemble into the correct CC dimers. In particular, human vimentin fragment D3 corresponding to the first half of coil2 (residues 261-335) stays monomeric in solution. We have induced its dimerization via introducing a disulfide link between two cysteines engineered in the hydrophobic core of the CC close to its N-terminus. The 2.3 Å crystal structure of the D3st (stabilized) fragment reveals a mostly parallel α-helical bundle structure in its N-terminal half which smoothly continues into a left-handed CC towards the C-terminus. This provides a direct evidence for a continuously α-helical structure of the coil2 segment and disproves the previously suggested existence of linker L2 separating it into two left-handed CCs. The general principles of CC dimer stabilization by disulfide introduction are also discussed." @default.
• W1995278329 created "2016-06-24" @default.
• W1995278329 creator A5006415661 @default.
• W1995278329 creator A5007438759 @default.
• W1995278329 date "2012-01-01" @default.
• W1995278329 modified "2023-09-26" @default.
• W1995278329 title "Stabilization of vimentin coil2 fragment via an engineered disulfide" @default.
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• W1995278329 doi "https://doi.org/10.1016/j.jsb.2011.11.014" @default.
• W1995278329 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/22119849" @default.
• W1995278329 hasPublicationYear "2012" @default.
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