5fds: Difference between revisions
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==Crystal structure of the monomeric allergen profilin (Hev b 8)== | |||
<StructureSection load='5fds' size='340' side='right' caption='[[5fds]], [[Resolution|resolution]] 1.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5fds]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FDS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FDS FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5fef|5fef]], [[5feg|5feg]]</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=5fds FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fds OCA], [http://pdbe.org/5fds PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fds RCSB], [http://www.ebi.ac.uk/pdbsum/5fds PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fds ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Oligomerization of allergens plays an important role in IgE-mediated reactions, as effective crosslinking of IgE- FcepsilonRI complexes on the cell membrane is dependent on the number of exposed B-cell epitopes in a single allergen molecule or on the occurrence of identical epitopes in a symmetrical arrangement. Few studies have attempted to experimentally demonstrate the connection between allergen dimerization and the ability to trigger allergic reactions. Here we studied plant allergenic profilins rHev b 8 (rubber tree) and rZea m 12 (maize) because they represent an important example of cross-reactivity in the latex-pollen-food syndrome. Both allergens in their monomeric and dimeric states were isolated and characterized by exclusion chromatography and mass spectrometry and were used in immunological in vitro experiments. Their crystal structures were solved, and for Hev b 8 a disulfide-linked homodimer was found. Comparing the structures we established that the longest loop is relevant for recognition by IgE antibodies, whereas the conserved regions are important for cross-reactivity. We produced a novel monoclonal murine IgE (mAb 2F5), specific for rHev b 8, which was useful to provide evidence that profilin dimerization considerably increases the IgE-mediated degranulation in rat basophilic leukemia cells. | |||
Structural insights into the IgE mediated responses induced by the allergens Hev b 8 and Zea m 12 in their dimeric forms.,Mares-Mejia I, Martinez-Caballero S, Garay-Canales C, Cano-Sanchez P, Torres-Larios A, Lara-Gonzalez S, Ortega E, Rodriguez-Romero A Sci Rep. 2016 Sep 2;6:32552. doi: 10.1038/srep32552. PMID:27586352<ref>PMID:27586352</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5fds" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Mares-Mejia, I]] | |||
[[Category: Rodriguez-Romero, A]] | [[Category: Rodriguez-Romero, A]] | ||
[[Category: | [[Category: Actin binding protein]] | ||
[[Category: Allergen]] | |||
[[Category: Allergy]] | |||
[[Category: Cross-reactivity]] | |||
[[Category: Hev b 8]] | |||
Revision as of 18:23, 14 September 2016
Crystal structure of the monomeric allergen profilin (Hev b 8)Crystal structure of the monomeric allergen profilin (Hev b 8)
Structural highlights
Publication Abstract from PubMedOligomerization of allergens plays an important role in IgE-mediated reactions, as effective crosslinking of IgE- FcepsilonRI complexes on the cell membrane is dependent on the number of exposed B-cell epitopes in a single allergen molecule or on the occurrence of identical epitopes in a symmetrical arrangement. Few studies have attempted to experimentally demonstrate the connection between allergen dimerization and the ability to trigger allergic reactions. Here we studied plant allergenic profilins rHev b 8 (rubber tree) and rZea m 12 (maize) because they represent an important example of cross-reactivity in the latex-pollen-food syndrome. Both allergens in their monomeric and dimeric states were isolated and characterized by exclusion chromatography and mass spectrometry and were used in immunological in vitro experiments. Their crystal structures were solved, and for Hev b 8 a disulfide-linked homodimer was found. Comparing the structures we established that the longest loop is relevant for recognition by IgE antibodies, whereas the conserved regions are important for cross-reactivity. We produced a novel monoclonal murine IgE (mAb 2F5), specific for rHev b 8, which was useful to provide evidence that profilin dimerization considerably increases the IgE-mediated degranulation in rat basophilic leukemia cells. Structural insights into the IgE mediated responses induced by the allergens Hev b 8 and Zea m 12 in their dimeric forms.,Mares-Mejia I, Martinez-Caballero S, Garay-Canales C, Cano-Sanchez P, Torres-Larios A, Lara-Gonzalez S, Ortega E, Rodriguez-Romero A Sci Rep. 2016 Sep 2;6:32552. doi: 10.1038/srep32552. PMID:27586352[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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