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7SD2

Murine Fab that recognizes Hev b 8 (profilin for Hevea brasiliensis)

Summary for 7SD2
Entry DOI10.2210/pdb7sd2/pdb
DescriptorHeavy Chain Antibody IgE/Fab anti-profilin Hev b 8, Light Chain Antibody IgE/Fab anti-profilin Hev b 8 (2 entities in total)
Functional Keywordsantibody, ige/fab fragment, immune system
Biological sourceMus musculus (Mouse)
More
Total number of polymer chains6
Total formula weight140526.99
Authors
Rodriguez-Romero, A.,Garcia-Ramirez, B. (deposition date: 2021-09-29, release date: 2022-08-10, Last modification date: 2024-10-16)
Primary citationGarcia-Ramirez, B.,Mares-Mejia, I.,Rodriguez-Hernandez, A.,Cano-Sanchez, P.,Torres-Larios, A.,Ortega, E.,Rodriguez-Romero, A.
A native IgE in complex with profilin provides insights into allergen recognition and cross-reactivity.
Commun Biol, 5:748-748, 2022
Cited by
PubMed Abstract: Allergies have become a rising health problem, where plentiful substances can trigger IgE-mediated allergies in humans. While profilins are considered minor allergens, these ubiquitous proteins are primary molecules involved in cross-reactivity and pollen-food allergy syndrome. Here we report the first crystal structures of murine Fab/IgE, with its chains naturally paired, in complex with the allergen profilin from Hevea brasiliensis (Hev b 8). The crystallographic models revealed that the IgE's six complementarity-determining regions (CDRs) interact with the allergen, comprising a rigid paratope-epitope surface of 926 Å, which includes an extensive network of interactions. Interestingly, we also observed previously unreported flexibility at Fab/IgE's elbow angle, which did not influence the shape of the paratope. The Fab/IgE exhibits a high affinity for Hev b 8, even when using 1 M NaCl in BLI experiments. Finally, based on the encouraging cross-reactivity assays using two mutants of the maize profilin (Zea m 12), this antibody could be a promising tool in IgE engineering for diagnosis and research applications.
PubMed: 35902770
DOI: 10.1038/s42003-022-03718-w
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.75 Å)
Structure validation

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数据于2025-06-25公开中

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