ArticleScientific reports2019
Structural and thermodynamic basis for the recognition of the substrate-binding cleft on hen egg lysozyme by a single-domain antibody.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed.
- Mechanistic interpretability of fine-tuned protein language models for nanobody thermostability prediction.Bioinformatics (Oxford, England) · 2026Article
- AVIDbase: A biologically accurate structural dataset of nanobody-antigen complexes.Protein science : a publication of the Protein Society · 2026Article
- Repertoire-scale antibody structural prediction informs therapeutic design.Science advances · 2026Article
- Convergent strategies for nanobody-mediated inhibition of an epoxide hydrolase.bioRxiv : the preprint server for biology · 2026Article
- Macromolecular dimensions of a synthetic polyelectrolyte as a factor in its interactions with protein and cells: desirability for longer chains.Journal of materials chemistry. B · 2026Article
- Nanobodies in biomedicine: from molecular characteristics to fabrication and clinical translation.Military Medical Research · 2026Review
- NanoBinder: a machine learning assisted nanobody binding prediction tool using Rosetta energy scores.Journal of cheminformatics · 2025Article
- EvoNB: A protein language model-based workflow for nanobody mutation prediction and optimization.Journal of pharmaceutical analysis · 2025Article
- The process using a synthetic library that generates multiple diverse human single domain antibodies.Antibody therapeutics · 2024Article
- Functional Divergence in the Affinity and Stability of Non-Canonical Cysteines and Non-Canonical Disulfide Bonds: Insights from a VHH and VNAR Study.International journal of molecular sciences · 2024Article
- Structural basis for the recognition of human hemoglobin by the heme-acquisition protein Shr from Streptococcus pyogenes.Scientific reports · 2024Article
- Immunopotentiating Polyphosphazene Delivery Systems: Supramolecular Self-Assembly and Stability in the Presence of Plasma Proteins.Molecular pharmaceutics · 2024Article
- Conformational features and interaction mechanisms of VProtein science : a publication of the Protein Society · 2023Article
- Combined Multiplexed Phage Display, High-Throughput Sequencing, and Functional Assays as a Platform for Identifying Modulatory VHHs Targeting the FSHR.International journal of molecular sciences · 2023Article
- Article
- Arginine cluster introduction on framework region in anti-lysozyme antibody improved association rate constant by changing conformational diversity of CDR loops.Protein science : a publication of the Protein Society · 2023Article
- Extract-Shaped Immune Repertoires as Source for Nanobody-Based Human IgE in Grass Pollen Allergy.Molecular biotechnology · 2023Article
- Fluorine-Functionalized Polyphosphazene Immunoadjuvant: Synthesis, Solution Behavior and In Vivo Potency.Molecules (Basel, Switzerland) · 2023Article
- Increasing the melting temperature of VHH with the in silico free energy score.Scientific reports · 2023Article
- Structural Characterization of Nanobodies during Germline Maturation.Biomolecules · 2023Article
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Single-domain antibodies (VHHs or nanobodies), developed from heavy chain-only antibodies of camelids, are gaining attention as next-generation therapeutic agents. Despite their small size, the high affinity and specificity displayed by VHHs for antigen molecules rival those of IgGs. How such small antibodies achieve that level of performance? Structural studies have revealed that VHHs tend to recognize concave surfaces of their antigens with high shape-complementarity. However, the energetic contribution of individual residues located at the binding interface has not been addressed in detail, obscuring the actual mechanism by which VHHs target the concave surfaces of proteins. Herein, we show that a VHH specific for hen egg lysozyme, D3-L11, not only displayed the characteristic binding of VHHs to a concave region of the surface of the antigen, but also exhibited a distribution of energetic hot-spots like those of IgGs and conventional protein-protein complexes. The highly preorganized and energetically compact interface of D3-L11 recognizes the concave epitope with high shape complementarity by the classical lock-and-key mechanism. Our results shed light on the fundamental basis by which a particular VHH accommodate to the concave surface of an antigens with high affinity in a specific manner, enriching the mechanistic landscape of VHHs.
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