View source for 3smh


==Crystal structure of major peanut allergen Ara h 1==
<StructureSection load='3smh' size='340' side='right'caption='[[3smh]], [[Resolution|resolution]] 2.43&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3smh]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Arachis_hypogaea Arachis hypogaea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SMH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SMH 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]] 2.433&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</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=3smh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3smh OCA], [https://pdbe.org/3smh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3smh RCSB], [https://www.ebi.ac.uk/pdbsum/3smh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3smh ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
Ara h 1, a 7S globulin, is one of the three major peanut allergens. We previously reported the crystallization of the core region of recombinant Ara h 1. Here, we present the crystal structure of the Ara h 1 core at a resolution of 2.43 A. We also assayed the Ara h 1 core thermal stability and compared its final structure against other 7S globulins. The Ara h 1 core has a thermal denaturation temperature of 88.3 degrees C and a structure that is very similar to other 7S globulins. Previously identified linear IgE epitopes were also mapped on the three-dimensional structure. Most linear epitopes were found in the extended loop domains and the coils between the N- and C-terminal modules, while others were found in the less accessible beta-sheets of the C-terminal core beta-barrel domain of each monomer. Most of these epitopes become either slightly or significantly buried upon trimer formation, implying that allergen digestion in the gut is required for these epitopes to be accessible to immunoglobulins. Our findings also suggest that both intact and partially degraded allergens should be employed in future diagnostic and immunotherapeutic strategies.

Crystal structure of the major peanut allergen Ara h 1.,Cabanos C, Urabe H, Tandang-Silvas MR, Utsumi S, Mikami B, Maruyama N Mol Immunol. 2011 Oct;49(1-2):115-23. Epub 2011 Sep 7. PMID:21903274<ref>PMID:21903274</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
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</StructureSection>
[[Category: Arachis hypogaea]]
[[Category: Large Structures]]
[[Category: Cabanos CS]]
[[Category: Maruyama N]]
[[Category: Mikami B]]