3mq1

<StructureSection load='3mq1' size='340' side='right' caption='[[3mq1]], [[Resolution|resolution]] 2.80&Aring;' scene=''>

<table><tr><td colspan='2'>[[3mq1]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Derpt Derpt]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MQ1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MQ1 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DERP5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6956 DERPT])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3mq1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mq1 OCA], [http://pdbe.org/3mq1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3mq1 RCSB], [http://www.ebi.ac.uk/pdbsum/3mq1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3mq1 ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

Group 5 allergens from house dust mites elicit strong IgE antibody binding in mite-allergic patients. The structure of Der p 5 was determined by x-ray crystallography to better understand the IgE epitopes, to investigate the biologic function in mites, and to compare with the conflicting published Blo t 5 structures, designated 2JMH and 2JRK in the Protein Data Bank. Der p 5 is a three-helical bundle similar to Blo t 5, but the interactions of the helices are more similar to 2JMH than 2JRK. The crystallographic asymmetric unit contains three dimers of Der p 5 that are not exactly alike. Solution scattering techniques were used to assess the multimeric state of Der p 5 in vitro and showed that the predominant state was monomeric, similar to Blo t 5, but larger multimeric species are also present. In the crystal, the formation of the Der p 5 dimer creates a large hydrophobic cavity of approximately 3000 A(3) that could be a ligand-binding site. Many allergens are known to bind hydrophobic ligands, which are thought to stimulate the innate immune system and have adjuvant-like effects on IgE-mediated inflammatory responses.

Der p 5 crystal structure provides insight into the group 5 dust mite allergens.,Mueller GA, Gosavi RA, Krahn JM, Edwards LL, Cuneo MJ, Glesner J, Pomes A, Chapman MD, London RE, Pedersen LC J Biol Chem. 2010 Aug 13;285(33):25394-401. Epub 2010 Jun 9. PMID:20534590<ref>PMID:20534590</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 3mq1" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Derpt]]

[[Category: Chapman, M D]]

[[Category: Cuneo, M J]]

[[Category: Edwards, L L]]

[[Category: Glesner, J]]

[[Category: Gosavi, R A]]

[[Category: Krahn, J M]]

[[Category: London, R E]]

[[Category: Mueller, G A]]

[[Category: Pedersen, L C]]

[[Category: Pomes, A]]

[[Category: Dust mite]]