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3MQ1

Crystal Structure of Dust Mite Allergen Der p 5

Summary for 3MQ1
Entry DOI10.2210/pdb3mq1/pdb
DescriptorMite allergen Der p 5, (4S)-2-METHYL-2,4-PENTANEDIOL, (4R)-2-METHYLPENTANE-2,4-DIOL, ... (5 entities in total)
Functional Keywordsallergen, dust mite
Biological sourceDermatophagoides pteronyssinus (European house dust mite)
Total number of polymer chains6
Total formula weight76971.55
Authors
Mueller, G.A.,Gosavi, R.A.,Krahn, J.M.,Edwards, L.L.,Cuneo, M.J.,Glesner, J.,Pomes, A.,Chapman, M.D.,London, R.E.,Pedersen, L.C. (deposition date: 2010-04-27, release date: 2010-06-02, Last modification date: 2024-02-21)
Primary citationMueller, G.A.,Gosavi, R.A.,Krahn, J.M.,Edwards, L.L.,Cuneo, M.J.,Glesner, J.,Pomes, A.,Chapman, M.D.,London, R.E.,Pedersen, L.C.
Der p 5 crystal structure provides insight into the group 5 dust mite allergens.
J.Biol.Chem., 285:25394-25401, 2010
Cited by
PubMed Abstract: 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.
PubMed: 20534590
DOI: 10.1074/jbc.M110.128306
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.8 Å)
Structure validation

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数据于2025-06-18公开中

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