ArticleStructure (London, England : 1993)2015
The membrane- and soluble-protein helix-helix interactome: similar geometry via different interactions.
Article in Structure (London, England : 1993), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed.
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- Designability of α-Helical Protein Filaments.Sub-cellular biochemistry · 2026Review
- Design principles of the common Gly-X6-Gly membrane protein building block.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- High-throughput discovery of transmembrane helix dimers from human single-pass membrane proteins with TOXGREEN sort-seq.PNAS nexus · 2025Article
- Sequence-dependent scale for translocon-mediated insertion of interfacial helices in membranes.Science advances · 2025Article
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- De novo-designed transmembrane proteins bind and regulate a cytokine receptor.Nature chemical biology · 2024Article
- Analysis and prediction of interactions between transmembrane and non-transmembrane proteins.BMC genomics · 2024Article
- Missense3D-TM: Predicting the Effect of Missense Variants in Helical Transmembrane Protein Regions Using 3D Protein Structures.Journal of molecular biology · 2024Article
- Thermodynamic analysis of the GASBiophysical journal · 2023Article
- 3D interaction homology: The hydrophobic residues alanine, isoleucine, leucine, proline and valine play different structural roles in soluble and membrane proteins.Frontiers in molecular biosciences · 2023Article
- Protein Design: From the Aspect of Water Solubility and Stability.Chemical reviews · 2022Review
- Spiers Memorial Lecture: Analysis andFaraday discussions · 2021Article
- Enumeration and comprehensive in-silico modeling of three-helix bundle structures composed of typical αα-hairpins.BMC bioinformatics · 2021Article
- Computational Simulation of Holin S105 in Membrane Bilayer and Its Dimerization Through a Helix-Turn-Helix Motif.The Journal of membrane biology · 2021Article
- Constructing ion channels from water-soluble α-helical barrels.Nature chemistry · 2021Article
- MENSAdb: a thorough structural analysis of membrane protein dimers.Database : the journal of biological databases and curation · 2021Article
- Structural analysis of cross α-helical nanotubes provides insight into the designability of filamentous peptide nanomaterials.Nature communications · 2021Article
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6 authors.
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Abstract
α Helices are a basic unit of protein secondary structure and therefore the interaction between helices is crucial to understanding tertiary and higher-order folds. Comparing subtle variations in the structural and sequence motifs between membrane and soluble proteins sheds light on the different constraints faced by each environment and elucidates the complex puzzle of membrane protein folding. Here, we demonstrate that membrane and water-soluble helix pairs share a small number of similar folds with various interhelical distances. The composition of the residues that pack at the interface between corresponding motifs shows that hydrophobic residues tend to be more enriched in the water-soluble class of structures and small residues in the transmembrane class. The latter group facilitates packing via sidechain- and backbone-mediated hydrogen bonds within the low-dielectric membrane milieu. The helix-helix interactome space, with its associated sequence preferences and accompanying hydrogen-bonding patterns, should be useful for engineering, prediction, and design of protein structure.
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