+Open data
-Basic information
Entry | Database: SASBDB / ID: SASDA94 |
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Sample | Der p21
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Biological species | Escherichia coli (E. coli) |
Citation | Journal: Allergy / Year: 2008 Title: Characterization of Der p 21, a new important allergen derived from the gut of house dust mites. Authors: M Weghofer / Y Dall'Antonia / M Grote / A Stöcklinger / M Kneidinger / N Balic / M-T Krauth / E Fernández-Caldas / W R Thomas / M van Hage / S Vieths / S Spitzauer / F Horak / D I Svergun ...Authors: M Weghofer / Y Dall'Antonia / M Grote / A Stöcklinger / M Kneidinger / N Balic / M-T Krauth / E Fernández-Caldas / W R Thomas / M van Hage / S Vieths / S Spitzauer / F Horak / D I Svergun / P V Konarev / P Valent / J Thalhamer / W Keller / R Valenta / S Vrtala / Abstract: BACKGROUND: The house dust mite (HDM) Dermatophagoides pteronyssinus is a major allergen source eliciting allergic asthma. The aim of the study was to identify new important HDM allergens associated with allergic asthma. METHODS: A cDNA coding for a new mite allergen, designated Der p 21, was isolated using immunoglobulin E (IgE) antibodies from patients with allergic asthma out of a D. pteronyssinus expression cDNA ...METHODS: A cDNA coding for a new mite allergen, designated Der p 21, was isolated using immunoglobulin E (IgE) antibodies from patients with allergic asthma out of a D. pteronyssinus expression cDNA library and expressed in Escherichia coli. RESULTS: Circular dichroism analysis of the purified allergen showed that rDer p 21 (14 726 Da) is one of the few mite allergens with an alpha-helical secondary structure. The protein exhibited high ...RESULTS: Circular dichroism analysis of the purified allergen showed that rDer p 21 (14 726 Da) is one of the few mite allergens with an alpha-helical secondary structure. The protein exhibited high thermal stability and refolding capacity, and, as determined by small angle X-ray scattering, formed a dimer consisting of two flat triangles. rDer p 21 bound high levels of patients' IgE antibodies and showed high allergenic activity in basophil activation experiments. Rabbit anti-Der p 21 IgG antibodies inhibited mite-allergic patients' IgE binding and allowed the ultrastructural localization of the allergen in the midgut (epithelium, lumen and faeces) of D. pteronyssinus by immunogold electron microscopy. Der p 21 revealed sequence homology with group 5 mite allergens, but IgE and IgG reactivity data and cross-inhibition studies identified it as a new mite allergen. CONCLUSIONS: Der p 21 is a new important mite allergen which is liberated into the environment via faecal particles and hence may be associated with allergic asthma. |
Contact author |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Models
Model #49 | Type: dummy / Software: dammin / Symmetry: P2 / Chi-square value: 3.493161 Search similar-shape structures of this assembly by Omokage search (details) |
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Model #50 | Type: mix / Software: Bunch / Radius of dummy atoms: 1.90 A / Symmetry: P2 / Chi-square value: 3.0625 Search similar-shape structures of this assembly by Omokage search (details) |
-Sample
Sample | Name: Der p21 / Sample MW: 26 kDa / Specimen concentration: 4.7 mg/ml |
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Buffer | Name: 10 mM Hepes / pH: 7 |
Entity #49 | Name: Derp21 / Type: protein / Description: Der p21, allegren / Formula weight: 13 / Num. of mol.: 2 / Source: Escherichia coli Sequence: MFIVGDKKED EWRMAFDRLM MEELETKIDQ VEKGLLHLSE QYKELEKTKS KELKEQILRE LTIGENFMKG ALKFFEMEAK RTDLNMFERY NYEFALESIK LLIKKLDELA KKVKAVNPDE YY |
-Experimental information
Beam | Instrument name: DORIS III X33 / City: Hamburg / 国: Germany / Type of source: X-ray synchrotron | |||||||||||||||||||||||||||
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Detector | Name: MAR 345 Image Plate | |||||||||||||||||||||||||||
Scan | Title: der p21 / Measurement date: Jul 24, 2006 / Storage temperature: 10 °C / Cell temperature: 10 °C / Exposure time: 120 sec. / Number of frames: 2 / Unit: 1/nm /
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Distance distribution function P(R) | Sofotware P(R): GNOM 4.5a / Number of points: 512 /
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Result | Type of curve: single_conc /
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