3MQ1: Crystal Structure of Dust Mite Allergen DER P 5

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.
PDB ID: 3MQ1Download
MMDB ID: 82517
PDB Deposition Date: 2010/4/27
Updated in MMDB: 2010/11
Experimental Method:
x-ray diffraction
Resolution: 2.8  Å
Source Organism:
Similar Structures:
Biological Unit for 3MQ1: hexameric; determined by software (PISA)
Molecular Components in 3MQ1
Label Count Molecule
Proteins (6 molecules)
Mite Allergen DER P 5
Molecule annotation
Chemicals (35 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB