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==A disulfide switch determines proteolytic resistance in the birch pollen allergen Bet v 2==
<StructureSection load='5nzc' size='340' side='right'caption='[[5nzc]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5nzc]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NZC OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5NZC FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5nzc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nzc OCA], [http://pdbe.org/5nzc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nzc RCSB], [http://www.ebi.ac.uk/pdbsum/5nzc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nzc ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/PROF2_BETPN PROF2_BETPN]] 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 (By similarity). 
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== Publication Abstract from PubMed ==
Birch pollen allergy affects more than 20% of the European allergic population. On a molecular level, birch pollen allergy can be linked to the two dominant allergens Bet v 1 and Bet v 2. Bet v 2 belongs to the profilin family, which is abundant in the plant kingdom. Importantly, the homologous plant profilins have a conserved cysteine motif with a currently unknown functional relevance. In particular, it is unknown whether the motif is relevant for disulfide formation and to what extent it would affect the profilins' structural, functional and immunological properties. Here we present crystal structures of Bet v 2 in the reduced and the oxidized state, i.e., without and with a disulfide bridge. Despite overall structural similarity, the two structures distinctly differ at their termini which are stabilized to each other in the oxidized, i.e., disulfide-linked state. These structural differences translate into differences in their proteolytic resistance. Whereas the oxidized Bet v 2 is rather resistant towards the endolysosomal protease cathepsin S, it is rapidly degraded in the reduced form. By contrast, both Bet v 2 forms exhibit similar immunological properties as evidenced by their binding to IgE antibodies from birch pollen allergic patients and by their ability to trigger histamine release in a humanized rat basophilic leukemia cells (RBL) assay, independent of the presence or absence of the disulfide bridge. Taken together our findings suggest that the oxidized Bet v 2 conformation should be the relevant species, with a much longer retention time to trigger immune responses.

Two Distinct Conformations in Bet v 2 Determine Its Proteolytic Resistance to Cathepsin S.,Soh WT, Briza P, Dall E, Asam C, Schubert M, Huber S, Aglas L, Bohle B, Ferreira F, Brandstetter H Int J Mol Sci. 2017 Oct 16;18(10). pii: E2156. doi: 10.3390/ijms18102156. PMID:29035299<ref>PMID:29035299</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
*[[Profilin 3D Structures|Profilin 3D Structures]]
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Brandstetter, H]]
[[Category: Soh, W T]]
[[Category: Allergen]]
[[Category: Bet v 2]]
[[Category: Profilin]]