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8G4P

Crystal structure of the peanut allergen Ara h 2 bound by two neutralizing antibodies 13T1 and 13T5

Summary for 8G4P
Entry DOI10.2210/pdb8g4p/pdb
Descriptor13t1 Fab heavy chain, 13T1 Fab light chain, 13T5 Fab heavy chain, ... (10 entities in total)
Functional Keywordsallergy, antibody, peanut, epitope, paratope, allergen
Biological sourceHomo sapiens (human)
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Total number of polymer chains5
Total formula weight113682.09
Authors
Pedersen, L.C.,Mueller, G.A.,Min, J. (deposition date: 2023-02-10, release date: 2023-12-20, Last modification date: 2024-10-09)
Primary citationMin, J.,Keswani, T.,LaHood, N.A.,Lytle, I.R.,Marini-Rapoport, O.,Andrieux, L.,Sneed, S.L.,Edwards, L.L.,Petrovich, R.M.,Perera, L.,Pomes, A.,Pedersen, L.C.,Patil, S.U.,Mueller, G.A.
Design of an Ara h 2 hypoallergen from conformational epitopes.
Clin Exp Allergy, 54:46-55, 2024
Cited by
PubMed Abstract: Adverse reactions are relatively common during peanut oral immunotherapy. To reduce the risk to the patient, some researchers have proposed modifying the allergen to reduce IgE reactivity, creating a putative hypoallergen. Analysis of recently cloned human IgG from patients treated with peanut immunotherapy suggested that there are three common conformational epitopes for the major peanut allergen Ara h 2. We sought to test if structural information on these epitopes could indicate mutagenesis targets for designing a hypoallergen and evaluated the reduction in IgE binding via immunochemistry and a mouse model of passive cutaneous anaphylaxis (PCA).
PubMed: 38168500
DOI: 10.1111/cea.14433
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.25 Å)
Structure validation

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