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3EBW

Crystal structure of major allergens, Per a 4 from cockroaches

Summary for 3EBW
Entry DOI10.2210/pdb3ebw/pdb
DescriptorPer a 4 allergen, 2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL (2 entities in total)
Functional Keywordsbeta barrel, allergen, cockroach
Biological sourcePeriplaneta americana (American cockroach)
Total number of polymer chains2
Total formula weight38152.17
Authors
Tan, Y.W.,Chan, S.L.,Chew, F.T.,Sivaraman, J.,Mok, Y.K. (deposition date: 2008-08-28, release date: 2008-12-02, Last modification date: 2024-10-16)
Primary citationTan, Y.W.,Chan, S.L.,Ong, T.C.,Yit, L.Y.,Tiong, Y.S.,Chew, F.T.,Sivaraman, J.,Mok, Y.K.
Structures of two major allergens, Bla g 4 and Per a 4, from cockroaches and their IgE binding epitopes.
J.Biol.Chem., 284:3148-3157, 2008
Cited by
PubMed Abstract: Inhalant allergens from cockroaches are an important cause of asthma to millions of individuals worldwide. Here we report for the first time the structures of two major cockroach allergens, Bla g 4 and Per a 4, that adopt a typical lipocalin fold but with distinct structural features as compared with other known lipocalin allergens. Both Bla g 4 and Per a 4 contain two long-range disulfide bonds linking the N and C termini to a beta-barrel. The C-terminal helix of Bla g 4 is bent and greatly extended toward the N terminus. Bla g 4 is found to be a monomer, whereas Per a 4 exists as a dimer in solution with a novel dimeric interface involving residues from loops at the top and bottom of the beta-barrel. Putative ligand binding sites of both allergens are determined by docking of the juvenile hormone III inside the beta-barrel and found to interact with the ligand using non-conserved residues. Bla g 4 and Per a 4 are found to be cross-reactive in sera IgE binding, at least in the Singaporean Chinese population tested. A major IgE binding epitope unique to Per a 4 is found on the loops at the bottom of the beta-barrel that may aid the development of hypoallergens for immunotherapy.
PubMed: 19056737
DOI: 10.1074/jbc.M807209200
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.8 Å)
Structure validation

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