ArticleNature communications2015
Atomic view of the histidine environment stabilizing higher-pH conformations of pH-dependent proteins.
Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Small-angle scattering studies on diverse peptide-based nanotube and helical ribbon structures reveal distinct form and structure factors.Journal of applied crystallography · 2025Article
- Cryo-EM structures of GnRHR: Foundations for next-generation therapeutics.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Nanofibrous Peptide Hydrogels Leveraging Histidine to Modulate pH-Responsive Supramolecular Assembly and Antibody Release.Biomacromolecules · 2025Article
- Missense variant analysis in the TRPV1 ARD reveals the unexpected functional significance of a methionine.PloS one · 2025Article
- Raman Multi-Omic Snapshot and Statistical Validation of Structural Differences between Herpes Simplex Type I and Epstein-Barr Viruses.International journal of molecular sciences · 2023Article
- Recent Experimental Advances in Characterizing the Self-Assembly and Phase Behavior of Polypeptoids.Materials (Basel, Switzerland) · 2023Review
- Caprin-1 binding to the critical stress granule protein G3BP1 is influenced by pH.Open biology · 2023Article
- Impact of structural dynamics on biological functions of flaviviruses.The FEBS journal · 2023Review
- Essential Role of Histidine for Rapid Copper(II)-Mediated Disassembly of Neurokinin B Amyloid.Biomolecules · 2022Article
- Aggregation Behavior of Structurally Similar Therapeutic Peptides Investigated byMolecular pharmaceutics · 2022Article
- Highly acidic pH facilitates enamel protein self-assembly, apatite crystal growth and enamel protein interactions in the early enamel matrix.Frontiers in physiology · 2022Article
- Multiscale Structural Elucidation of Peptide Nanotubes by X-Ray Scattering Methods.Frontiers in bioengineering and biotechnology · 2021Review
- Activity and Mechanism of Action of the Bioceramic Silicon Nitride as an Environmentally Friendly Alternative for the Control of the Grapevine Downy Mildew PathogenFrontiers in microbiology · 2020Article
- Modulation of μ-opioid receptor activation by acidic pH is dependent on ligand structure and an ionizable amino acid residue.British journal of pharmacology · 2019Article
- General lack of structural characterization of chemically synthesized long peptides.Protein science : a publication of the Protein Society · 2019Review
- ZnScientific reports · 2018Article
- Structural resolution of inorganic nanotubes with complex stoichiometry.Nature communications · 2018Article
Corrections and comments
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Authors and funding
16 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
External stimuli are powerful tools that naturally control protein assemblies and functions. For example, during viral entry and exit changes in pH are known to trigger large protein conformational changes. However, the molecular features stabilizing the higher pH structures remain unclear. Here we elucidate the conformational change of a self-assembling peptide that forms either small or large nanotubes dependent on the pH. The sub-angstrom high-pH peptide structure reveals a globular conformation stabilized through a strong histidine-serine H-bond and a tight histidine-aromatic packing. Lowering the pH induces histidine protonation, disrupts these interactions and triggers a large change to an extended β-sheet-based conformation. Re-visiting available structures of proteins with pH-dependent conformations reveals both histidine-containing aromatic pockets and histidine-serine proximity as key motifs in higher pH structures. The mechanism discovered in this study may thus be generally used by pH-dependent proteins and opens new prospects in the field of nanomaterials.
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