View source for 2as8


==Crystal structure of mature and fully active Der p 1 allergen==
<StructureSection load='2as8' size='340' side='right'caption='[[2as8]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2as8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Dermatophagoides_pteronyssinus Dermatophagoides pteronyssinus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AS8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AS8 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2as8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2as8 OCA], [https://pdbe.org/2as8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2as8 RCSB], [https://www.ebi.ac.uk/pdbsum/2as8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2as8 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PEPT1_DERPT PEPT1_DERPT] Thiol protease, with a preference for substrates with a large hydrophobic side chain in the P2 position, or with basic residues.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/as/2as8_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2as8 ConSurf].
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== Publication Abstract from PubMed ==
BACKGROUND: Der p 1 is a 25-kd allergen with cysteine protease activity. Sensitization to Der p 1 affects a large proportion of individuals with allergy, resulting in rhinitis, asthma, and/or atopic dermatitis. OBJECTIVE: We determined the Der p 1 crystallographic structure to understand the relationships among structure, function, and allergenicity. METHODS: Recombinant pro-Der p 1 was produced in Pichia pastoris and allowed to mature spontaneously before purification by a 2-step procedure. Protease activity was checked by using a fluorogenic peptide substrate. Allergenicity was analysed by IgE binding assays and basophil activation test. The determination of the 3-dimensional structure was obtained by X-ray crystallography at 1.9 A resolution. RESULTS: The recombinant protein is fully active and expresses an allergenicity equivalent to its natural counterpart. Der p 1 exhibits a cysteine protease fold typical of the papain family, has a magnesium binding site, and forms dimers with a large interface. The crystal lattice shows that the dimers are tightly packed in a compact double layer of proteins. Such an assembly likely exists in dry fecal pellets, the natural form of allergen exposure, and appears ideal to interact with cell surface and trigger allergic inflammation. CONCLUSION: We present here the 3-dimensional structural features of mature fully active Der p 1, one of the main allergens involved in human allergic diseases. This opens the possibility to evaluate the importance of enzymatic activity in pathology and possible new therapeutic interventions.

Three-dimensional structure and IgE-binding properties of mature fully active Der p 1, a clinically relevant major allergen.,de Halleux S, Stura E, VanderElst L, Carlier V, Jacquemin M, Saint-Remy JM J Allergy Clin Immunol. 2006 Mar;117(3):571-6. Epub 2006 Jan 30. PMID:16522455<ref>PMID:16522455</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Dermatophagoides pteronyssinus]]
[[Category: Large Structures]]
[[Category: Carlier V]]
[[Category: Jacquemin M]]
[[Category: Saint-Remy J-M]]
[[Category: Stura E]]
[[Category: VanderElst L]]
[[Category: De Halleux S]]