7uv4

Pis v 3.0101 vicilin leader sequence residues 56-115

spinqualitylabelsall models 7uv4 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7uv4 is a 1 chain structure with sequence from Pistacia vera. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function VCL_PISVE Publication Abstract from PubMed Peanut and tree-nut allergies are frequently comorbid for reasons not completely understood. Vicilin-buried peptides (VBPs) are an emerging family of food allergens whose conserved structural fold could mediate peanut/tree-nut co-allergy. Peptide microarrays were used to identify immunoglobulin E (IgE) epitopes from the N-terminus of the vicilin allergens Ara h 1, Ana o 1, Jug r 2, and Pis v 3 using serum from three patient diagnosis groups: monoallergic to either peanuts or cashew/pistachio, or dual allergic. IgE binding peptides were highly prevalent in the VBP domains AH1.1, AO1.1, JR2.1, and PV3.1, but not in AO1.2, JR2.2, JR2.3, and PV3.2 nor the unstructured regions. The IgE profiles did not correlate with diagnosis group. The structure of the VBPs from cashew and pistachio was solved using solution-NMR. Comparisons of structural features suggest that the VBP scaffold from peanuts and tree-nuts can support cross-reactivity. This may help understand comorbidity and cross-reactivity despite a distant evolutionary origin. Structure and IgE Cross-Reactivity among Cashew, Pistachio, Walnut, and Peanut Vicilin-Buried Peptides.,Foo ACY, Nesbit JB, Gipson SAY, DeRose EF, Cheng H, Hurlburt BK, Kulis MD, Kim EH, Dreskin SC, Mustafa S, Maleki SJ, Mueller GA J Agric Food Chem. 2023 Feb 15;71(6):2990-2998. doi: 10.1021/acs.jafc.2c07061. , Epub 2023 Feb 2. PMID:36728846 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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