3s7i

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<StructureSection load='3s7i' size='340' side='right'caption='[[3s7i]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
<StructureSection load='3s7i' size='340' side='right'caption='[[3s7i]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3s7i]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arahy Arahy]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3S7I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3S7I FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3s7i]] is a 2 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=3S7I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3S7I FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</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]] 2.35&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3s7e|3s7e]]</div></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=CL:CHLORIDE+ION'>CL</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=3s7i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s7i OCA], [https://pdbe.org/3s7i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3s7i RCSB], [https://www.ebi.ac.uk/pdbsum/3s7i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3s7i ProSAT]</span></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=3s7i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s7i OCA], [https://pdbe.org/3s7i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3s7i RCSB], [https://www.ebi.ac.uk/pdbsum/3s7i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3s7i ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/ALL12_ARAHY ALL12_ARAHY]
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Allergic reactions to peanuts and tree nuts are major causes of anaphylaxis in the United States. We compare different properties of natural and recombinant versions of Ara h 1, a major peanut allergen, through structural, immunologic, and bioinformatics analyses. Small angle x-ray scattering studies show that natural Ara h 1 forms higher molecular weight aggregates in solution. In contrast, the full-length recombinant protein is partially unfolded and exists as a monomer. The crystal structure of the Ara h 1 core (residues 170-586) shows that the central part of the allergen has a bicupin fold, which is in agreement with our bioinformatics analysis. In its crystalline state, the core region of Ara h 1 forms trimeric assemblies, while in solution the protein exists as higher molecular weight assemblies. This finding reveals that the residues forming the core region of the protein are sufficient for formation of Ara h 1 trimers and higher order oligomers. Natural and recombinant variants of proteins tested in in vitro gastric and duodenal digestion assays show that the natural protein is the most stable form, followed by the recombinant Ara h 1 core fragment and the full-length recombinant protein. Additionally, IgE binding studies reveal that the natural and recombinant allergens have different patterns of interaction with IgE antibodies. The molecular basis of cross-reactivity between vicilin allergens is also elucidated.
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Structural and Immunologic Characterization of Ara h 1, a Major Peanut Allergen.,Chruszcz M, Maleki SJ, Majorek KA, Demas M, Bublin M, Solberg R, Hurlburt BK, Ruan S, Mattisohn CP, Breiteneder H, Minor W J Biol Chem. 2011 Nov 11;286(45):39318-27. Epub 2011 Sep 14. PMID:21917921<ref>PMID:21917921</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 3s7i" style="background-color:#fffaf0;"></div>
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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]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Chruszcz, M]]
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[[Category: Chruszcz M]]
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[[Category: Maleki, S J]]
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[[Category: Maleki SJ]]
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[[Category: Minor, W]]
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[[Category: Minor W]]
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[[Category: Solberg, R]]
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[[Category: Solberg R]]
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[[Category: Allergen]]
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[[Category: Bicupin]]
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[[Category: Storage seed protein]]
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[[Category: Vicilin]]
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Current revision

Crystal structure of Ara h 1

PDB ID 3s7i

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