ArticleProceedings of the National Academy of Sciences of the United States of America1998
An autonomous folding unit mediates the assembly of two-stranded coiled coils.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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Who cites it
53 citing papers in PubMed.
- High-pH NMR to Identify Macromolecular Hydrogen-Bonds and Foldons.Journal of the American Chemical Society · 2026Article
- High-pH NMR to Identify Macromolecular Hydrogen-Bonds and Foldons.bioRxiv : the preprint server for biology · 2026Article
- Controlling oncogenic KRAS signaling pathways with a Palladium-responsive peptide.Communications chemistry · 2022Article
- Water-mediated interactions destabilize proteins.Protein science : a publication of the Protein Society · 2021Article
- Membrane Binding and Homodimerization of Atg16 Via Two Distinct Protein Regions is Essential for Autophagy in Yeast.Journal of molecular biology · 2021Article
- Crystal and solution structures reveal oligomerization of individual capsid homology domains of Drosophila Arc.PloS one · 2021Article
- Distribution of disease-causing germline mutations in coiled-coils implies an important role of their N-terminal region.Scientific reports · 2020Article
- Stu2 uses a 15-nm parallel coiled coil for kinetochore localization and concomitant regulation of the mitotic spindle.Molecular biology of the cell · 2018Article
- Design considerations in coiled-coil fusion constructs for the structural determination of a problematic region of the human cardiac myosin rod.Journal of structural biology · 2017Article
- Structural basis for the regulatory interactions of proapoptotic Par-4.Cell death and differentiation · 2017Article
- Nuclear Magnetic Resonance Structures of GCN4p Are Largely Conserved When Ion Pairs Are Disrupted at Acidic pH but Show a Relaxation of the Coiled Coil Superhelix.Biochemistry · 2017Article
- The Structure and Topology of α-Helical Coiled Coils.Sub-cellular biochemistry · 2017Review
- Molecular studies on structural changes and oligomerisation of violaxanthin de-epoxidase associated with the pH-dependent activation.Photosynthesis research · 2016Article
- Article
- The Elucidation of the Interactome of 16 Arabidopsis bZIP Factors Reveals Three Independent Functional Networks.PloS one · 2015Article
- Sequence-resolved free energy profiles of stress-bearing vimentin intermediate filaments.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Effectiveness of a novel immunogenic nanoparticle platform for Toxoplasma peptide vaccine in HLA transgenic mice.Vaccine · 2014Article
- The tripartite motif coiled-coil is an elongated antiparallel hairpin dimer.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Article
- Polymorphism in tropomyosin structure and function.Journal of muscle research and cell motility · 2013Review
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Subunit oligomerization of many proteins is mediated by coiled-coil domains. Although the basic features contributing to the thermodynamic stability of coiled coils are well understood, the mechanistic details of their assembly have not yet been dissected. Here we report a 13-residue sequence pattern that occurs with limited sequence variations in many two-stranded coiled coils and that is absolutely required for the assembly of the Dictyostelium discoideum actin-bundling protein cortexillin I and the yeast transcriptional activator GCN4. The functional relationship between coiled-coil "trigger" sequences was manifested by replacing the intrinsic trigger motif of GCN4 with the related sequence from cortexillin I. We demonstrate that these trigger sequences represent autonomous helical folding units that, in contrast to arbitrarily chosen heptad repeats, can mediate coiled-coil formation. Aside from being of general interest for protein folding, trigger motifs should be of particular importance in the protein de novo design.
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