ArticleFrontiers in immunology2022
Structural Features of Antibody-Peptide Recognition.
Article in Frontiers in immunology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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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.
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Who cites it
20 citing papers in PubMed, 25 citations in OpenAlex.
- PDBe-SIFTS: An open-source tool for Structure Integration with Function, Taxonomy, and Sequences, featuring improved alignment, scoring scheme, and accelerated search.Protein science : a publication of the Protein Society · 2026Article
- TINA: a geometry-aware post-hoc scoring framework for protein-protein interaction.Acta pharmacologica Sinica · 2026Article
- Pre-Clinical Development of Two DNA Vaccines Encoding MrkA of Klebsiella pneumoniae: Effect of Plasmid Backbone on Immunogenicity and Protective Efficacy Against Sepsis.Microbial biotechnology · 2026Article
- Structural similarity between CD38 and the Duffy antigen as a potential mechanism of attenuated anti-Fy antibody reactivity with soluble CD38.British journal of haematology · 2026Article
- Benchmarking AlphaFold and related deep learning approaches for modeling antibody and TCR antigen recognition.bioRxiv : the preprint server for biology · 2026Article
- DeepRank-Ab: a scoring function for antibody-antigen complexes based on geometric deep learning.Communications biology · 2026Article
- PDBe-SIFTS: an open-source tool for Structure Integration with Function, Taxonomy, and Sequences, featuring improved alignment, scoring scheme, and accelerated search.bioRxiv : the preprint server for biology · 2026Article
- Dynamic changes in serum HER2-peptide-specific autoantibodies predict response to neoadjuvant therapy in HER2-positive breast cancer.Breast cancer research : BCR · 2026Article
- GPA33 forms a distinct diagnostic target class to Claudin 18.2 in oesophageal adenocarcinoma enabling the development of a novel GPA33 antibody-based detection platform.Cellular & molecular biology letters · 2026Article
- Long-range allosteric communication within antibodies affects antigen-binding affinity.Frontiers in immunology · 2026Article
- Cross-neutralising antibodies to SARS-CoV-2 in sera from straw-coloured fruit bats (Eidolon helvum) in Nigeria.BMC veterinary research · 2025Article
- Design of intrinsically disordered region binding proteins.Science (New York, N.Y.) · 2025Article
- RosettaHDX: Predicting antibody-antigen interaction from hydrogen-deuterium exchange mass spectrometry data.Journal of structural biology · 2025Article
- Molecular convergence of neutralizing antibodies in human revealed by repeated rabies vaccination.NPJ vaccines · 2025Article
- Structural trends in antibody-antigen binding interfaces: a computational analysis of 1833 experimentally determined 3D structures.Computational and structural biotechnology journal · 2024Article
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- Glycylglycine promotes the solubility and antigenic utility of recombinant HCV structural proteins in a point-of-care immunoassay for detection of active viremia.Microbial cell factories · 2024Article
- Evaluation of AlphaFold antibody-antigen modeling with implications for improving predictive accuracy.Protein science : a publication of the Protein Society · 2024Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
Antibody recognition of antigens is a critical element of adaptive immunity. One key class of antibody-antigen complexes is comprised of antibodies targeting linear epitopes of proteins, which in some cases are conserved elements of viruses and pathogens of relevance for vaccine design and immunotherapy. Here we report a detailed analysis of the structural and interface features of this class of complexes, based on a set of nearly 200 nonredundant high resolution antibody-peptide complex structures that were assembled from the Protein Data Bank. We found that antibody-bound peptides adopt a broad range of conformations, often displaying limited secondary structure, and that the same peptide sequence bound by different antibodies can in many cases exhibit varying conformations. Propensities of contacts with antibody loops and extent of antibody binding conformational changes were found to be broadly similar to those for antibodies in complex with larger protein antigens. However, antibody-peptide interfaces showed lower buried surface areas and fewer hydrogen bonds than antibody-protein antigen complexes, while calculated binding energy per buried interface area was found to be higher on average for antibody-peptide interfaces, likely due in part to a greater proportion of buried hydrophobic residues and higher shape complementarity. This dataset and these observations can be of use for future studies focused on this class of interactions, including predictive computational modeling efforts and the design of antibodies or epitope-based vaccine immunogens.
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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.