Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Prediction of hypervariable CDR-H3 loop structures in antibodies

M Reczko1, A C Martin, H Bohr

  • 1Molecular Biophysics Department, German Cancer Research Center, Heidelberg.

Protein Engineering
|April 1, 1995
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

AI-derived therapeutic development of a serotonin receptor-targeting drug for the treatment of opioid use disorder.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same author

Seismic resurfacing of 433 Eros indicative of a highly dissipative interior for large near-Earth asteroids.

Nature astronomy·2025
Same author

Benzannulation and Hydrocarboxylation Methods for the Synthesis of a Neopentylene-Fused Analogue of Ibuprofen.

ACS omega·2021
Same author

Synthesis of <i>gem</i>-Dimethylcyclopentane-Fused Arenes with Various Topologies via TBD-Mediated Dehydro-Diels-Alder Reaction.

The Journal of organic chemistry·2021
Same author

Inhibition of Ophiognomonia clavigignenti-juglandacearum by Juglans Species Bark Extracts.

Plant disease·2019
Same author

Neuroprotection requires the functions of the RNA-binding protein HuR.

Cell death and differentiation·2014
Same journal

Structure of a human Rhinovirus complexed with its receptor molecule.

Protein engineering·2024
Same journal

pH-responsive polymer-assisted refolding of urea- and organic solvent-denatured alpha-chymotrypsin.

Protein engineering·2004
Same journal

Evaluation of different linker regions for multimerization and coupling chemistry for immobilization of a proteinaceous affinity ligand.

Protein engineering·2004
Same journal

Recombinant porcine intestinal carboxylesterase: cloning from the pig liver esterase gene by site-directed mutagenesis, functional expression and characterization.

Protein engineering·2004
Same journal

Periplasmic expression of human growth hormone via plasmid vectors containing the lambdaPL promoter: use of HPLC for product quantification.

Protein engineering·2004
Same journal

Shift of fibril-forming ability of the designed alpha-helical coiled-coil peptides into the physiological pH region.

Protein engineering·2004
See all related articles

This study predicts antibody hypervariable loop structures using artificial neural networks. The novel method accurately models CDR-H3 loops up to 17 residues from sequence alone.

Area of Science:

  • Immunoinformatics
  • Structural Biology
  • Computational Chemistry

Background:

  • Antibody hypervariable loops, particularly CDR-H3, are crucial for antigen binding but challenging to model due to their high variability.
  • Accurate structural prediction of these loops is essential for antibody engineering and drug design.

Purpose of the Study:

  • To develop a novel computational method for predicting the three-dimensional structure of CDR-H3 loops solely from their amino acid sequences.
  • To extend structural prediction capabilities to longer CDR-H3 loops (up to 17 residues).

Main Methods:

  • Utilized artificial neural networks trained on a comprehensive dataset of CDR-H3-like loops from the Brookhaven Protein Databank.
  • Modeled loop structures by predicting backbone dihedral angles (phi and psi) for each residue.

Related Experiment Videos

  • Validated predictions against experimentally determined structures for unique CDR-H3 loops.

    • Main Results:

    • Achieved accurate predictions for CDR-H3 loop structures, including lengths up to 17 residues.
    • Demonstrated an average root mean square deviation of 2.65 Å in Cartesian coordinates for 21 unique CDR-H3 loop predictions.
    • The neural network approach showed high fidelity in predicting dihedral angles.

    Conclusions:

    • The developed artificial neural network method provides a robust approach for predicting CDR-H3 loop structures from sequence.
    • This method significantly advances the structural prediction of antibody complementarity determining regions.
    • Integration with existing modeling protocols enhances the utility for antibody structural analysis and design.