From Proteopedia
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| | {{STRUCTURE_1xkg| PDB=1xkg | SCENE= }} | | {{STRUCTURE_1xkg| PDB=1xkg | SCENE= }} |
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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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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_16148130}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 16148130 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_16148130}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Major allergen]] | | [[Category: Major allergen]] |
| | [[Category: Pro peptide]] | | [[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 Sun Jul 27 14:57:31 2008'' |
Revision as of 11:57, 27 July 2008
Template:STRUCTURE 1xkg
Crystal structure of the major house dust mite allergen Der p 1 in its pro form at 1.61 A resolution
Template:ABSTRACT PUBMED 16148130
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 Sun Jul 27 14:57:31 2008
