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==2.70 A crystal structure of the Amb a 11 cysteine protease, a major ragweed pollen allergen, in its proform==
<StructureSection load='5egw' size='340' side='right'caption='[[5egw]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5egw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ambrosia_artemisiifolia Ambrosia artemisiifolia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EGW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5EGW 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]] 2.7&#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=5egw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5egw OCA], [https://pdbe.org/5egw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5egw RCSB], [https://www.ebi.ac.uk/pdbsum/5egw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5egw ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CEP01_AMBAR CEP01_AMBAR] Cysteine protease. Hydrolyzes casein and synthetic peptide Boc-Val-Leu-Lys-7-amino-4-methylcoumarin (Boc-VLK-AMC) in vitro.<ref>PMID:25865353</ref> <ref>PMID:27129273</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Allergy to the short ragweed (Ambrosia artemisiifolia) pollen is a major health problem. The ragweed allergen repertoire has been recently expanded with the identification of Amb a 11, a new major allergen belonging to the cysteine protease family. To better characterize Amb a 11, a recombinant proform of the molecule with a preserved active site was produced in Escherichia coli, refolded and processed in vitro into a mature enzyme. The enzymatic activity is revealed by maturation, following an autocatalytic processing resulting in the cleavage of both N- and C-terminal propeptides. The 2.05 A resolution crystal structure of pro-Amb a 11 shows an overall typical C1A cysteine protease fold, with a network of molecular interactions between the N-terminal propeptide and the catalytic triad of the enzyme. The allergenicity of Amb a 11 was confirmed in a murine sensitization model, resulting in airway inflammation, production of serum IgEs as well as induction of Th2 immune responses. Of note, inflammatory responses were higher with the mature form, demonstrating that the cysteine protease activity critically contributes to the allergenicity of the molecule. Collectively, our results clearly demonstrate that Amb a 11 is a bona fide cysteine protease exhibiting a strong allergenicity. As such, it should be considered as an important molecule for diagnosis and immunotherapy of ragweed pollen allergy.

Structural and Functional Characterization of the Major Allergen Amb a 11 from Short Ragweed Pollen.,Groeme R, Airouche S, Kopecny D, Jaekel J, Savko M, Berjont N, Bussieres L, Le Mignon M, Jagic F, Zieglmayer P, Baron-Bodo V, Bordas-Le Floch V, Mascarell L, Briozzo P, Moingeon P J Biol Chem. 2016 Apr 19. pii: jbc.M115.702001. PMID:27129273<ref>PMID:27129273</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5egw" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Ambrosia artemisiifolia]]
[[Category: Large Structures]]
[[Category: Briozzo P]]
[[Category: Kopecny D]]