1xkg
From Proteopedia
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|PDB= 1xkg |SIZE=350|CAPTION= <scene name='initialview01'>1xkg</scene>, resolution 1.61Å | |PDB= 1xkg |SIZE=350|CAPTION= <scene name='initialview01'>1xkg</scene>, resolution 1.61Å | ||
|SITE= | |SITE= | ||
- | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=YT3:YTTRIUM+(III)+ION'>YT3</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= DERP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6956 Dermatophagoides pteronyssinus]) | |GENE= DERP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6956 Dermatophagoides pteronyssinus]) | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY= | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xkg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xkg OCA], [http://www.ebi.ac.uk/pdbsum/1xkg PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1xkg RCSB]</span> | ||
}} | }} | ||
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[[Category: Meno, K.]] | [[Category: Meno, K.]] | ||
[[Category: Thorsted, P B.]] | [[Category: Thorsted, P B.]] | ||
- | [[Category: GOL]] | ||
- | [[Category: SO4]] | ||
- | [[Category: YT3]] | ||
[[Category: cysteine protease]] | [[Category: cysteine protease]] | ||
[[Category: dermatophagoides pteronyssinus]] | [[Category: dermatophagoides pteronyssinus]] | ||
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[[Category: pro peptide]] | [[Category: pro peptide]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:50:51 2008'' |
Revision as of 21:50, 30 March 2008
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, resolution 1.61Å | |||||||
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Ligands: | , , | ||||||
Gene: | DERP1 (Dermatophagoides pteronyssinus) | ||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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
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