ArticleProtein science : a publication of the Protein Society2005
Structure of a shark IgNAR antibody variable domain and modeling of an early-developmental isotype.
Article in Protein science : a publication of the Protein Society, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed.
- In vitro selection of VNAR antibodies using bioinformatics-based library design and cDNA display.Biotechnology reports (Amsterdam, Netherlands) · 2026Article
- Nanobodies: From Discovery to AI-Driven Design.Biology · 2025Review
- A Single-Domain VNAR Nanobody Binds with High-Affinity and Selectivity to the Heparin Pentasaccharide Fondaparinux.International journal of molecular sciences · 2025Article
- VNAR: shark single-domain antibodies for the new era of medical biotechnology.Frontiers in immunology · 2025Review
- vNARs as Neutralizing Intracellular Therapeutic Agents: Glioblastoma as a Target.Antibodies (Basel, Switzerland) · 2024Review
- Review
- Shark IgNAR: The Next Broad Application Antibody in Clinical Diagnoses and Tumor Therapies?Marine drugs · 2023Review
- Therapeutic Antibodies in Medicine.Molecules (Basel, Switzerland) · 2023Review
- Targeting the Brain with Single-Domain Antibodies: Greater Potential Than Stated So Far?International journal of molecular sciences · 2023Review
- Screening and characterization of inhibitory vNAR targeting nanodisc-assembled influenza M2 proteins.iScience · 2023Article
- Construction of Semisynthetic Shark vNAR Yeast Surface Display Antibody Libraries.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Single domain antibodies derived from ancient animals as broadly neutralizing agents for SARS-CoV-2 and other coronaviruses.Biomedical engineering advances · 2022Review
- Ig-VAE: Generative modeling of protein structure by direct 3D coordinate generation.PLoS computational biology · 2022Article
- Identification of Anti-TNFα VNAR Single Domain Antibodies from Whitespotted Bambooshark (Marine drugs · 2022Article
- Research progress on unique paratope structure, antigen binding modes, and systematic mutagenesis strategies of single-domain antibodies.Frontiers in immunology · 2022Review
- A comprehensive comparison between camelid nanobodies and single chain variable fragments.Biomarker research · 2021Review
- Central Nervous System Delivery of Antibodies and Their Single-Domain Antibodies and Variable Fragment Derivatives with Focus on Intranasal Nose to Brain Administration.Antibodies (Basel, Switzerland) · 2021Review
- Broad Reactivity Single Domain Antibodies against Influenza Virus and Their Applications to Vaccine Potency Testing and Immunotherapy.Biomolecules · 2021Review
- On Origin and Evolution of the Antibody Molecule.Biology · 2021Review
- The immunoglobulins of cartilaginous fishes.Developmental and comparative immunology · 2021Review
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The new antigen receptor (IgNAR) antibodies from sharks are disulphide bonded dimers of two protein chains, each containing one variable and five constant domains. Three types of IgNAR variable domains have been discovered, with Type 3 appearing early in shark development and being overtaken by the antigen-driven affinity-matured Type 1 and 2 response. Here, we have determined the first structure of a naturally occurring Type 2 IgNAR variable domain, and identified the disulphide bond that links and stabilizes the CDR1 and CDR3 loops. This disulphide bridge locks the CDR3 loop in an "upright" conformation in contrast to other shark antibody structures, where a more lateral configuration is observed. Further, we sought to model the Type 3 isotype based on the crystallographic structure reported here. This modeling indicates (1) that internal Type 3-specific residues combine to pack into a compact immunoglobulin core that supports the CDR loop regions, and (2) that despite apparent low-sequence variability, there is sufficient plasticity in the CDR3 loop to form a conformationally diverse antigen-binding surface.
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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.