4b9r

From Proteopedia

(Difference between revisions)

Revision as of 20:02, 4 August 2016

Crystal structure of the Major Birch Pollen Allergen Bet v 1.0101 (isoform a) nitrated in vitro with tetranitromethan.

Structural highlights

4b9r is a 1 chain structure with sequence from Betpn. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:
Related:	1b6f, 1btv, 1bv1, 1fsk, 1llt, 1qmr, 4a80, 4a81, 4a83, 4a84, 4a85, 4a86, 4a87, 4a88, 4a8g
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[BEV1A_BETPN] May be a general steroid carrier protein (By similarity).

Publication Abstract from PubMed

Allergy prevalence has increased in industrialized countries. One contributing factor could be pollution, which can cause nitration of allergens exogenously (in the air) or endogenously (in inflamed lung tissue). We investigated the impact of nitration on both the structural and immunological behavior of the major birch pollen allergen Bet v 1.0101 to determine whether nitration might be a factor in the increased incidence of allergy. Bet v 1.0101 was nitrated with tetranitromethane. Immune effects were assessed by measuring the proliferation of specific T-cell lines (TCLs) upon stimulation with different concentrations of nitrated and unmodified allergen, and by measurement of cytokine release of monocyte-derived dendritic cells (moDCs) and primary DCs (primDCs) stimulated with nitrated versus unmodified allergen. HPLC-MS, crystallography, gel electrophoresis, amino acid analysis, size exclusion chromatography and molecular dynamics simulation were performed to characterize structural changes after nitration of the allergen. The proliferation of specific TCLs was higher upon stimulation with the nitrated allergen in comparison to the unmodified allergen. An important structural consequence of nitration was oligomerization. Moreover, analysis of the crystal structure of nitrated Bet v 1.0101 showed that amino acid residue Y83, located in the hydrophobic cavity, was nitrated to 100%. Both moDCs and primDCs showed decreased production of TH1-priming cytokines, thus favoring a TH2 response. These results implicate that nitration of Bet v 1.0101 might be a contributing factor to the observed increase in birch pollen allergy, and emphasize the importance of protein modifications in understanding the molecular basis of allergenicity.

The Impact of Nitration on the Structure and Immunogenicity of the Major Birch Pollen Allergen Bet v 1.0101.,Ackaert C, Kofler S, Horejs-Hoeck J, Zulehner N, Asam C, von Grafenstein S, Fuchs JE, Briza P, Liedl KR, Bohle B, Ferreira F, Brandstetter H, Oostingh GJ, Duschl A PLoS One. 2014 Aug 15;9(8):e104520. doi: 10.1371/journal.pone.0104520., eCollection 2014. PMID:25126882^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Ackaert C, Kofler S, Horejs-Hoeck J, Zulehner N, Asam C, von Grafenstein S, Fuchs JE, Briza P, Liedl KR, Bohle B, Ferreira F, Brandstetter H, Oostingh GJ, Duschl A. The Impact of Nitration on the Structure and Immunogenicity of the Major Birch Pollen Allergen Bet v 1.0101. PLoS One. 2014 Aug 15;9(8):e104520. doi: 10.1371/journal.pone.0104520., eCollection 2014. PMID:25126882 doi:http://dx.doi.org/10.1371/journal.pone.0104520

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4b9r"

@@ Line 1: / Line 1: @@
 ==Crystal structure of the Major Birch Pollen Allergen Bet v 1.0101 (isoform a) nitrated in vitro with tetranitromethan.==
 <StructureSection load='4b9r' size='340' side='right' caption='[[4b9r]], [[Resolution|resolution]] 1.76&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NIY:META-NITRO-TYROSINE'>NIY</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1b6f|1b6f]], [[1btv|1btv]], [[1bv1|1bv1]], [[1fsk|1fsk]], [[1llt|1llt]], [[1qmr|1qmr]], [[4a80|4a80]], [[4a81|4a81]], [[4a83|4a83]], [[4a84|4a84]], [[4a85|4a85]], [[4a86|4a86]], [[4a87|4a87]], [[4a88|4a88]], [[4a8g|4a8g]]</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=4b9r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b9r OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4b9r RCSB], [http://www.ebi.ac.uk/pdbsum/4b9r PDBsum]</span></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=4b9r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b9r OCA], [http://pdbe.org/4b9r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4b9r RCSB], [http://www.ebi.ac.uk/pdbsum/4b9r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4b9r ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 19: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4b9r" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

4b9r

From Proteopedia

Revision as of 20:02, 4 August 2016

Crystal structure of the Major Birch Pollen Allergen Bet v 1.0101 (isoform a) nitrated in vitro with tetranitromethan.

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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