5fds: Difference between revisions

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== Function ==
== Function ==
[https://www.uniprot.org/uniprot/PROF2_HEVBR PROF2_HEVBR]  
[https://www.uniprot.org/uniprot/PROF2_HEVBR PROF2_HEVBR]  
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== 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
==See Also==
*[[Profilin 3D Structures|Profilin 3D Structures]]
*[[Profilin 3D Structures|Profilin 3D Structures]]
== References ==
<references/>
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Latest revision as of 15:31, 6 March 2024

Crystal structure of the monomeric allergen profilin (Hev b 8)Crystal structure of the monomeric allergen profilin (Hev b 8)

Structural highlights

5fds is a 1 chain structure with sequence from Hevea brasiliensis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PROF2_HEVBR

See Also

5fds, resolution 1.90Å

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA