1xkg
From Proteopedia
(New page: 200px<br /><applet load="1xkg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xkg, resolution 1.61Å" /> '''Crystal structure of...) |
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| - | [[Image:1xkg.gif|left|200px]]<br /><applet load="1xkg" size=" | + | [[Image:1xkg.gif|left|200px]]<br /><applet load="1xkg" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1xkg, resolution 1.61Å" /> | caption="1xkg, resolution 1.61Å" /> | ||
'''Crystal structure of the major house dust mite allergen Der p 1 in its pro form at 1.61 A resolution'''<br /> | '''Crystal structure of the major house dust mite allergen Der p 1 in its pro form at 1.61 A resolution'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Allergy to house dust mite is among the most prevalent allergic diseases | + | 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== | ==About this Structure== | ||
| - | 1XKG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Dermatophagoides_pteronyssinus Dermatophagoides pteronyssinus] with YT3, SO4 and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1XKG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Dermatophagoides_pteronyssinus Dermatophagoides pteronyssinus] with <scene name='pdbligand=YT3:'>YT3</scene>, <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XKG OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Gajhede, M.]] | [[Category: Gajhede, M.]] | ||
[[Category: Meno, K.]] | [[Category: Meno, K.]] | ||
| - | [[Category: Thorsted, P | + | [[Category: Thorsted, P B.]] |
[[Category: GOL]] | [[Category: GOL]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
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[[Category: pro peptide]] | [[Category: pro peptide]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:55:45 2008'' |
Revision as of 13:55, 21 February 2008
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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
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 with , and as ligands. 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
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