3mq1

Publication Abstract from PubMed

Group 5 allergens from house dust mites elicit strong IgE antibody binding in mite-allergic patients. The structure of Der p 5 was determined by x-ray crystallography to better understand the IgE epitopes, to investigate the biologic function in mites, and to compare with the conflicting published Blo t 5 structures, designated 2JMH and 2JRK in the Protein Data Bank. Der p 5 is a three-helical bundle similar to Blo t 5, but the interactions of the helices are more similar to 2JMH than 2JRK. The crystallographic asymmetric unit contains three dimers of Der p 5 that are not exactly alike. Solution scattering techniques were used to assess the multimeric state of Der p 5 in vitro and showed that the predominant state was monomeric, similar to Blo t 5, but larger multimeric species are also present. In the crystal, the formation of the Der p 5 dimer creates a large hydrophobic cavity of approximately 3000 A(3) that could be a ligand-binding site. Many allergens are known to bind hydrophobic ligands, which are thought to stimulate the innate immune system and have adjuvant-like effects on IgE-mediated inflammatory responses.

Der p 5 crystal structure provides insight into the group 5 dust mite allergens.,Mueller GA, Gosavi RA, Krahn JM, Edwards LL, Cuneo MJ, Glesner J, Pomes A, Chapman MD, London RE, Pedersen LC J Biol Chem. 2010 Aug 13;285(33):25394-401. Epub 2010 Jun 9. PMID:20534590^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.