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4esp

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==Crystal Structure of Peanut Allergen Ara h 5==
==Crystal Structure of Peanut Allergen Ara h 5==
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<StructureSection load='4esp' size='340' side='right' caption='[[4esp]], [[Resolution|resolution]] 1.10&Aring;' scene=''>
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<StructureSection load='4esp' size='340' side='right'caption='[[4esp]], [[Resolution|resolution]] 1.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4esp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arahy Arahy]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ESP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ESP FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4esp]] is a 1 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=4ESP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ESP FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.1&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">profilin ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3818 ARAHY])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene></td></tr>
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<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=4esp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4esp OCA], [http://pdbe.org/4esp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4esp RCSB], [http://www.ebi.ac.uk/pdbsum/4esp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4esp ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4esp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4esp OCA], [https://pdbe.org/4esp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4esp RCSB], [https://www.ebi.ac.uk/pdbsum/4esp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4esp ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/D3K177_ARAHY D3K177_ARAHY]] Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations.[RuleBase:RU003908]
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[https://www.uniprot.org/uniprot/D3K177_ARAHY D3K177_ARAHY] Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations.[RuleBase:RU003908]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Profilins from numerous species are known to be allergens, including food allergens, such as peanut ( Arachis hypogaea ) allergen Ara h 5, and pollen allergens, such as birch allergen Bet v 2. Patients with pollen allergy can also cross-react to peanut. Structural characterization of allergens will allow a better understanding of the allergenicity of food allergens and their cross-reactivities. The three-dimensional structures of most known food allergens remain to be elucidated. Here, we report the first crystallographic study of a food allergen in the profilin family. The structure of peanut allergen Ara h 5 was determined, and the resolution of the final refined structure was 1.1 A. Structure alignment revealed that Ara h 5 is more similar to Bet v 2 than to Hev b 8, although sequence alignment suggested that Ara h 5 is more closely related to Hev b 8 than to Bet v 2, indicating that homology-model-based prediction of immunoglobulin E epitopes needs to be interpreted with caution.
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Crystal Structure of Peanut ( Arachis hypogaea ) Allergen Ara h 5.,Wang Y, Fu TJ, Howard A, Kothary MH, McHugh TH, Zhang Y J Agric Food Chem. 2013 Feb 20;61(7):1573-8. doi: 10.1021/jf303861p. Epub 2013, Feb 11. PMID:23350842<ref>PMID:23350842</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4esp" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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*[[Profilin|Profilin]]
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*[[Profilin 3D Structures|Profilin 3D Structures]]
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Arahy]]
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[[Category: Arachis hypogaea]]
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[[Category: Wang, Y]]
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[[Category: Large Structures]]
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[[Category: Zhang, Y Z]]
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[[Category: Wang Y]]
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[[Category: Allergen]]
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[[Category: Zhang YZ]]
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[[Category: Allergy]]
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[[Category: Ara h 5]]
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[[Category: Peanut allergen]]
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[[Category: Profilin]]
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Current revision

Crystal Structure of Peanut Allergen Ara h 5

PDB ID 4esp

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