Der p 5 Crystal Structure Provides Insight into the Group 5 Dust Mite Allergens

作者：Mueller Geoffrey A^*; Gosavi Rajendrakumar A; Krahn Joseph M; Edwards Lori L; Cuneo Matthew J; Glesner Jill; Pomes Anna; Chapman Martin D; London Robert E; Pedersen Lars C

来源：JOURNAL OF BIOLOGICAL CHEMISTRY, 2010, 285(33): 25394-25401.

DOI：10.1074/jbc.M110.128306

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 crystallo-graphic 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 similar to 3000 angstrom(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.

• 出版日期2010-8-13