The crystal structure of recombinant proDer p 1, a major house dust mite proteolytic allergen.

@article{Meno2005TheCS,
  title={The crystal structure of recombinant proDer p 1, a major house dust mite proteolytic allergen.},
  author={K{\aa}re H Meno and Peter B. Thorsted and Henrik Ipsen and Ole Kristensen and J\orgen Nedergaard Larsen and Michael Dho Spangfort and Michael Gajhede and Kaare Lund},
  journal={Journal of immunology},
  year={2005},
  volume={175 6},
  pages={3835-45}
}
Allergy to house dust mite is among the most prevalent allergic diseases worldwide. Most house dust mite allergic patients react to Der p 1 from Dermatophagoides pteronyssinus, which is a cysteine protease. To avoid heterogeneity in the sample used for crystallization, a modified recombinant molecule was produced. The sequence of the proDer p 1 allergen was modified to reduce glycosylation and to abolish enzymatic activity. The resulting rproDer p 1 preparation was homogenous and stable and… CONTINUE READING

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