1xkg
From Proteopedia
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'''Crystal structure of the major house dust mite allergen Der p 1 in its pro form at 1.61 A resolution''' | '''Crystal structure of the major house dust mite allergen Der p 1 in its pro form at 1.61 A resolution''' | ||
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[[Category: Meno, K.]] | [[Category: Meno, K.]] | ||
[[Category: Thorsted, P B.]] | [[Category: Thorsted, P B.]] | ||
| - | [[Category: | + | [[Category: Cysteine protease]] |
| - | [[Category: | + | [[Category: Dermatophagoides pteronyssinus]] |
| - | [[Category: | + | [[Category: House dust mite]] |
| - | [[Category: | + | [[Category: Inactive mutant]] |
| - | [[Category: | + | [[Category: Major allergen]] |
| - | [[Category: | + | [[Category: Pro peptide]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:08:40 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 12:08, 3 May 2008
Crystal structure of the major house dust mite allergen Der p 1 in its pro form at 1.61 A resolution
Overview
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 yielded crystals diffracting to a resolution of 1.61 A. The active site is located in a large cleft on the surface of the molecule. The 80-aa pro-peptide adopts a unique fold that interacts with the active site cleft and a substantial adjacent area on the mature region, excluding access to the cleft and the active site. Studies performed using crossed-line immunoelectrophoresis and IgE inhibition experiments indicated that several epitopes are covered by the pro-peptide and that the epitopes on the recombinant mature molecule are indistinguishable from those on the natural one. The structure confirms previous results suggesting a preference for aliphatic residues in the important P2 position in substrates. Sequence variations in related species are concentrated on the surface, which explains the existence of cross-reacting and species-specific antibodies. This study describes the first crystal structure of one of the clinically most important house dust mite allergens, the cysteine protease Der p 1.
About this Structure
1XKG is a Single protein structure of sequence from Dermatophagoides pteronyssinus. Full crystallographic information is available from OCA.
Reference
The crystal structure of recombinant proDer p 1, a major house dust mite proteolytic allergen., Meno K, Thorsted PB, Ipsen H, Kristensen O, Larsen JN, Spangfort MD, Gajhede M, Lund K, J Immunol. 2005 Sep 15;175(6):3835-45. PMID:16148130 Page seeded by OCA on Sat May 3 15:08:40 2008
