ArticleProceedings of the National Academy of Sciences of the United States of America2015
High-resolution structures of a heterochiral coiled coil.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
21 citing papers in PubMed.
- Rapid clearance of achiral small-molecule drugs using de novo-designed proteins and their cyclic and mirror-image variants.Nature biomedical engineering · 2025Article
- Chirality Effects in Peptide-Based Dynamic Combinatorial Chemistry.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Design of an abiotic unimolecular three-helix bundle.Chemical science · 2025Article
- Accurate de novo design of heterochiral protein-protein interactions.Cell research · 2024Article
- Designing Coiled Coils for Heterochiral Complexation to Enhance Binding and Enzymatic Stability.Biomacromolecules · 2024Article
- MSL1 Promotes Liver Regeneration by Driving Phase Separation of STAT3 and Histone H4 and Enhancing Their Acetylation.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023Article
- Roles of inter- and intramolecular tryptophan interactions in membrane-active proteins revealed by racemic protein crystallography.Communications chemistry · 2023Article
- An abiotic, tetrameric, eight-helix bundle.Chemical science · 2023Article
- D-Peptide and D-Protein Technology: Recent Advances, Challenges, and Opportunities.Chembiochem : a European journal of chemical biology · 2023Review
- De novo design of discrete, stable 3Nature · 2022Article
- Biomaterials via peptide assembly: Design, characterization, and application in tissue engineering.Acta biomaterialia · 2022Review
- Chiral Selectivity of Secondary Nucleation in Amyloid Fibril Propagation.Angewandte Chemie (International ed. in English) · 2021Article
- Conformational interplay in hybrid peptide-helical aromatic foldamer macrocycles.Chemical science · 2021Article
- The folding propensity of α/sulfono-γ-AA peptidic foldamers with both left- and right-handedness.Communications chemistry · 2021Article
- Parallel Homochiral and Anti-Parallel Heterochiral Hydrogen-Bonding Interfaces in Multi-Helical Abiotic Foldamers.Angewandte Chemie (International ed. in English) · 2020Article
- Retention of Native Quaternary Structure in Racemic Melittin Crystals.Journal of the American Chemical Society · 2019Article
- A Hendecad Motif Is Preferred for Heterochiral Coiled-Coil Formation.Journal of the American Chemical Society · 2019Article
- Heterochiral Knottin Protein: Folding and Solution Structure.Biochemistry · 2017Article
- Optimizing side chains for crystal growth from water: a case study of aromatic amide foldamers.Chemical science · 2017Article
- Surfactant-facilitated crystallisation of water-soluble foldamers.Chemical science · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
12 authors.
Funding
Abstract
Interactions between polypeptide chains containing amino acid residues with opposite absolute configurations have long been a source of interest and speculation, but there is very little structural information for such heterochiral associations. The need to address this lacuna has grown in recent years because of increasing interest in the use of peptides generated from d amino acids (d peptides) as specific ligands for natural proteins, e.g., to inhibit deleterious protein-protein interactions. Coiled-coil interactions, between or among α-helices, represent the most common tertiary and quaternary packing motif in proteins. Heterochiral coiled-coil interactions were predicted over 50 years ago by Crick, and limited experimental data obtained in solution suggest that such interactions can indeed occur. To address the dearth of atomic-level structural characterization of heterochiral helix pairings, we report two independent crystal structures that elucidate coiled-coil packing between l- and d-peptide helices. Both structures resulted from racemic crystallization of a peptide corresponding to the transmembrane segment of the influenza M2 protein. Networks of canonical knobs-into-holes side-chain packing interactions are observed at each helical interface. However, the underlying patterns for these heterochiral coiled coils seem to deviate from the heptad sequence repeat that is characteristic of most homochiral analogs, with an apparent preference for a hendecad repeat pattern.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.