38DC

X-ray Structure of the FAB Fragment of a GluA2-specific Murine Monoclonal Antibody 15F1

Summary for 38DC

• Entry DOI: 10.2210/pdb38dc/pdb
• Descriptor: 15F1 Fab heavy chain, 15F1 Fab light chain (3 entities in total)
• Functional Keywords: fab fragment, antibody, glua2, immune system
• Biological source: Spodoptera frugiperda; More
• Total number of polymer chains: 4
• Total formula weight: 97770.61

Authors

Nix, J.,Dhandapani, G.,Spangler, C.J.,Pruneda, J.N.,Gouaux, E. (deposition date: 2026-08-20, release date: 2026-11-04)

Primary citation

Spangler, C.J.,Dhandapani, G.,Matsui, A.,Shiltseva, E.V.,Nix, J.,Pruneda, J.N.,Elferich, J.,Gouaux, E.
Programmable gold nanoparticle conjugates enable precise AMPA receptor localization at brain synapses by cryo-ET.
Biorxiv, 2026

PubMed Abstract: Cryo-electron tomography (cryo-ET) is a powerful approach to image cells, organelles, viruses and molecular assemblies. However, resolving smaller complexes and molecules is challenging and presents a roadblock to the broad application of cryo-ET. Gold nanoparticles (AuNPs) have been used to localize otherwise unidentifiable molecules and complexes in tomograms but are typically tethered to the target of interest via a flexible linker. As a result, the position of the AuNP does not directly define the location of the target. Here we attach AuNPs to Fab antibody fragments via cysteine residues on defined elements of secondary structure and show that the AuNPs are rigidly bound to the Fab. We use these Fab-AuNP conjugates to locate AMPA receptors and probe their conformation upon desensitization with sub nanometer resolution in tomograms derived from brain slice lamella. By harnessing small, homogeneous AuNPs with precise conjugation to a Fab, we have developed reagents that enable direct investigation of conformational states of previously unidentifiable biomolecules and complexes in tomograms.

PubMed: 42892767
DOI: 10.64898/2026.09.18.752772

Experimental method

X-RAY DIFFRACTION (2.5 Å)