View source for 9rtg


==Crystal structure of Ara h 2 immunocomplex with IgE Fab fragment==
<StructureSection load='9rtg' size='340' side='right'caption='[[9rtg]], [[Resolution|resolution]] 3.19&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9rtg]] is a 14 chain structure with sequence from [https://en.wikipedia.org/wiki/Arachis_hypogaea Arachis hypogaea] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9RTG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9RTG 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]] 3.19&#8491;</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=9rtg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9rtg OCA], [https://pdbe.org/9rtg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9rtg RCSB], [https://www.ebi.ac.uk/pdbsum/9rtg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9rtg ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CONG7_ARAHY CONG7_ARAHY] Weak inhibitor of trypsin.<ref>PMID:12847498</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
BACKGROUND: Peanut allergy is a serious form of food allergy that can lead to anaphylactic reactions. Research has shown that the Ara h 2 allergen is immunodominant and associated with fatal systemic reactions. METHODS: We determined the crystal structure of recombinant Ara h 2.0201 in a complex with the human-derived PA12P3D08 (D08) IgE Fab fragment at 3.2 A resolution. In addition, native mass spectrometry was used to study interactions of D08 with Ara h 2 and its peptides. RESULTS: The structure revealed that D08 Fab binds to a long loop of Ara h 2.0201, which contains three repeated DPYSPS motifs. The immunocomplex structure illustrated how three copies of D08 Fabs can bind simultaneously to Ara h 2.0201 in close proximity. Native mass spectrometry studies of D08 Fab with Ara h 2.0201 and peptides containing 2-3 motifs demonstrated cross-linking of Ara h 2.0201 in solution and the propensity of D08 Fab to self-associate. Motif peptides from Ara h 2.0201 highlighted the importance of proline hydroxylation for binding affinity. D08 Fab also bound to hydroxyproline-containing peptides from Ara h 1 and 3. CONCLUSIONS: The trivalent binding is effective in forming large allergen-IgE complexes on mast cell or basophil surfaces and contributes to the potency of Ara h 2 in triggering allergic reactions and highlighting its role in anaphylaxis. Proline hydroxylation considerably enhances D08 binding affinity and contributes to cross-reactivity among Ara h 1-3 allergens.

Structural Basis for Trivalent Cross-Linking of a Patient-Derived IgE Antibody by the Major Peanut Allergen Ara h 2.0201.,Parkkinen T, Heiniluoto H, Janis J, Takkinen K, Rouvinen J Allergy. 2026 Jun;81(6):2036-2046. doi: 10.1111/all.70258. Epub 2026 Feb 17. PMID:41700105<ref>PMID:41700105</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9rtg" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Arachis hypogaea]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Parkkinen T]]
[[Category: Rouvinen J]]