ArticleStructure (London, England : 1993)2015
The origin of CDR H3 structural diversity.
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 56 papers.
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Who cites it
56 citing papers in PubMed.
- The Evolution of Artificial Intelligence in Antibody Design: From Structure-Based Engineering to Generative Models.Antibodies (Basel, Switzerland) · 2026Review
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- Phage Display Technology: Design, Library Construction, and Panning Strategies for Antibody Development.Biomolecules & therapeutics · 2026Review
- Characterising nanobody developability to improve therapeutic design using the Therapeutic Nanobody Profiler.Communications biology · 2026Article
- Antibody Affinity Maturation by Computational Design.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Protein sequence modelling with Bayesian flow networks.Nature communications · 2025Article
- Unveiling Interaction Signatures Across Viral Pathogens through VASCO: Viral Antigen-Antibody Structural COmplex dataset.bioRxiv : the preprint server for biology · 2025Article
- Improved prediction of antibody and their complexes with clustered generative modelling ensembles.Bioinformatics advances · 2025Article
- Determining key residues of engineered scFv antibody variants with improved MMP-9 binding using deep sequencing and machine learning.Computational and structural biotechnology journal · 2024Article
- De Novo Synthesis and Structural Elucidation of CDR-H3 Loop Mimics.ACS chemical biology · 2024Article
- Development of Anti-OSCAR Antibodies for the Treatment of Osteoarthritis.Biomedicines · 2023Article
- Structure and Dynamics Guiding Design of Antibody Therapeutics and Vaccines.Antibodies (Basel, Switzerland) · 2023Review
- Article
- VHH CDR-H3 conformation is determined by VH germline usage.Communications biology · 2023Article
- Defining and Studying B Cell Receptor and TCR Interactions.Journal of immunology (Baltimore, Md. : 1950) · 2023Article
- Structural Classification of CDR-H3 in Single-Domain VMethods in molecular biology (Clifton, N.J.) · 2023Article
- Specific attributes of the VFrontiers in immunology · 2023Article
- Physicochemical differences between camelid single-domain antibodies and mammalian antibodies.Turkish journal of biology = Turk biyoloji dergisi · 2023Article
- Unveiling the affinity-stability relationship in anti-measles virus antibodies: a computational approach for hotspots prediction.Frontiers in molecular biosciences · 2023Article
- Predicting phenotype transition probabilities via conditional algorithmic probability approximations.Journal of the Royal Society, Interface · 2022Article
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3 authors.
Funding
Abstract
Antibody complementarity determining region (CDR) H3 loops are critical for adaptive immunological functions. Although the other five CDR loops adopt predictable canonical structures, H3 conformations have proven unclassifiable, other than an unusual C-terminal "kink" present in most antibodies. To determine why the majority of H3 loops are kinked and to learn whether non-antibody proteins have loop structures similar to those of H3, we searched a set of 15,679 high-quality non-antibody structures for regions geometrically similar to the residues immediately surrounding the loop. By incorporating the kink into our search, we identified 1,030 H3-like loops from 632 protein families. Some protein families, including PDZ domains, appear to use the identified region for recognition and binding. Our results suggest that the kink is conserved in the immunoglobulin heavy chain fold because it disrupts the β-strand pairing at the base of the loop. Thus, the kink is a critical driver of the observed structural diversity in CDR H3.
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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.