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Cited by 136Protein Structure and DynamicsChemical Synthesis and AnalysisRNA and protein synthesis mechanisms

The DOI matches its Crossref record; 61 of the 61 references it cites were found in a registry or an index.

Molecular basis of coiled-coil formation

Open access
Steinmetz, Michel O., Jelesarov, Ilian, Matousek, William M., Honnappa, Srinivas, Jahnke, Wolfgang, Missimer, John H., Frank, Sabine, Alexandrescu, Andrei T., Kammerer, Richard A.·2007·Proceedings of the National Academy of Sciences
DOI 10.1073/pnas.0700321104PMC PMC1855353
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Abstract

Coiled coils have attracted considerable interest as design templates in a wide range of applications. Successful coiled-coil design strategies therefore require a detailed understanding of coiled-coil folding. One common feature shared by coiled coils is the presence of a short autonomous helical folding unit, termed “trigger sequence,” that is indispensable for folding. Detailed knowledge of trigger sequences at the molecular level is thus key to a general understanding of coiled-coil formation. Using a multidisciplinary approach, we identify and characterize here the molecular determinants that specify the helical conformation of the monomeric early folding intermediate of the GCN4 coiled coil. We demonstrate that a network of hydrogen-bonding and electrostatic interactions stabilize the trigger-sequence helix. This network is rearranged in the final dimeric coiled-coil structure, and its destabilization significantly slows down GCN4 leucine zipper folding. Our findings provide a general explanation for the molecular mechanism of coiled-coil formation.

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Metadata

Authors
Steinmetz, M. O., Jelesarov, I., Matousek, W. M., Honnappa, S., Jahnke, W., Missimer, J. H., Frank, S., Alexandrescu, A. T., & Kammerer, R. A.
Affiliations
  • Paul Scherrer Institute (CH)
  • University of Zurich (CH)
  • University of Connecticut (US)
  • *Biomolecular Research, Structural Biology, Paul Scherrer Institut, CH-5232 Villigen PSI, Switzerland;
  • Novartis (Switzerland) (CH)
  • F. Hoffmann-La Roche AG (CH)
  • Wellcome Centre for Cell-Matrix Research (GB)
ORCID
Venue
Proceedings of the National Academy of Sciences
Publisher
National Academy of Sciences
Published
2007-04-24
Volume
104
Issue
17
Pages
7062-7067
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
DOI
10.1073/pnas.0700321104
PMC
PMC1855353
OpenAlex
W2032892814
Cited by
136
References
61
Citations by year
2026: 2 · 2025: 6 · 2024: 9 · 2022: 1 · 2021: 2 · 2020: 5 · 2019: 3 · 2018: 4 · 2017: 7 · 2016: 5 · 2015: 7 · 2014: 10 · 2013: 13 · 2012: 15
FWCI
4.91
Type
journal article
Language
en
Open access
Locations
  • Proceedings of the National Academy of Sciences (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
  • DORA PSI (Paul Scherrer Institute) (submittedVersion)
  • Research Explorer (The University of Manchester) (submittedVersion)
Funders
  • Wellcome Trust
  • Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (109423)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
  • Physical Sciences › Chemistry › Organic Chemistry › Chemical Synthesis and Analysis
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
Keywords
GCN4, leucine zipper, helix stabilization, hydrogen bonding, electrostatic interactions, protein folding mechanism, dimerization
MeSH terms
Arginine, DNA-Binding Proteins, Hydrogen-Ion Concentration, Kinetics, Magnetic Resonance Spectroscopy, Peptides, Solutions, Thermodynamics, Transcription Factors, Leucine Zippers, Protein Folding, Amino Acid Substitution, Saccharomyces cerevisiae Proteins, Mutant Proteins, Basic-Leucine Zipper Transcription Factors

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