4hpg

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{{STRUCTURE_4hpg| PDB=4hpg | SCENE= }}
 
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===Crystal structure of a glycosylated beta-1,3-glucanase (HEV B 2), an allergen from Hevea brasiliensis===
 
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{{ABSTRACT_PUBMED_24531467}}
 
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==About this Structure==
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==Crystal structure of a glycosylated beta-1,3-glucanase (HEV B 2), an allergen from Hevea brasiliensis==
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[[4hpg]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Hevea_brasiliensis Hevea brasiliensis]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3em5 3em5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HPG OCA].
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<StructureSection load='4hpg' size='340' side='right' caption='[[4hpg]], [[Resolution|resolution]] 2.54&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4hpg]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Hevea_brasiliensis Hevea brasiliensis]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3em5 3em5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HPG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HPG FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene></td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucan_endo-1,3-beta-D-glucosidase Glucan endo-1,3-beta-D-glucosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.39 3.2.1.39] </span></td></tr>
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<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=4hpg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hpg OCA], [http://pdbe.org/4hpg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4hpg RCSB], [http://www.ebi.ac.uk/pdbsum/4hpg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4hpg ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Endogenous glycosylated Hev b 2 (endo-beta-1,3-glucanase) from Hevea brasiliensis is an important latex allergen that is recognized by IgE antibodies from patients who suffer from latex allergy. The carbohydrate moieties of Hev b 2 constitute a potentially important IgE-binding epitope that could be responsible for its cross-reactivity. Here, the structure of the endogenous isoform II of Hev b 2 that exhibits three post-translational modifications, including an N-terminal pyroglutamate and two glycosylation sites at Asn27 and at Asn314, is reported from two crystal polymorphs. These modifications form a patch on the surface of the molecule that is proposed to be one of the binding sites for IgE. A structure is also proposed for the most important N-glycan present in this protein as determined by digestion with specific enzymes. To analyze the role of the carbohydrate moieties in IgE antibody binding and in human basophil activation, the glycoallergen was enzymatically deglycosylated and evaluated. Time-lapse automated video microscopy of basophils stimulated with glycosylated Hev b 2 revealed basophil activation and degranulation. Immunological studies suggested that carbohydrates on Hev b 2 represent an allergenic IgE epitope. In addition, a dimer was found in each asymmetric unit that may reflect a regulatory mechanism of this plant defence protein.
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Structural analysis of the endogenous glycoallergen Hev b 2 (endo-beta-1,3-glucanase) from Hevea brasiliensis and its recognition by human basophils.,Rodriguez-Romero A, Hernandez-Santoyo A, Fuentes-Silva D, Palomares LA, Munoz-Cruz S, Yepez-Mulia L, Orozco-Martinez S Acta Crystallogr D Biol Crystallogr. 2014 Feb;70(Pt 2):329-41. doi:, 10.1107/S1399004713027673. Epub 2014 Jan 29. PMID:24531467<ref>PMID:24531467</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4hpg" style="background-color:#fffaf0;"></div>
==See Also==
==See Also==
*[[Glucanase|Glucanase]]
*[[Glucanase|Glucanase]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:024531467</ref><references group="xtra"/><references/>
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__TOC__
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</StructureSection>
[[Category: Glucan endo-1,3-beta-D-glucosidase]]
[[Category: Glucan endo-1,3-beta-D-glucosidase]]
[[Category: Hevea brasiliensis]]
[[Category: Hevea brasiliensis]]
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[[Category: Hernandez-Santoyo, A.]]
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[[Category: Hernandez-Santoyo, A]]
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[[Category: Rodriguez-Romero, A.]]
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[[Category: Rodriguez-Romero, A]]
[[Category: Allergen]]
[[Category: Allergen]]
[[Category: Carbohydrate/sugar binding]]
[[Category: Carbohydrate/sugar binding]]

Revision as of 13:40, 11 August 2016

Crystal structure of a glycosylated beta-1,3-glucanase (HEV B 2), an allergen from Hevea brasiliensis

4hpg, resolution 2.54Å

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