View source for 4qip


==Crystal Structure of Major Birch Pollen Allergen Bet v 1 isoform a in complex with Sodium Dodecyl Sulfate==
<StructureSection load='4qip' size='340' side='right'caption='[[4qip]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4qip]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Betula_pendula Betula pendula]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QIP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QIP 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&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SDS:DODECYL+SULFATE'>SDS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=4qip FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qip OCA], [https://pdbe.org/4qip PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qip RCSB], [https://www.ebi.ac.uk/pdbsum/4qip PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qip ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/BEV1A_BETPN BEV1A_BETPN] May be a general steroid carrier protein (By similarity).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Pathogenesis-related plant proteins of class-10 (PR-10) are essential for storage and transport of small molecules. A prominent member of the PR-10 family, the major birch pollen allergen Bet v 1, is the main cause of spring pollinosis in the temperate climate zone of the northern hemisphere. Bet v 1 binds various ligand molecules to its internal cavity, and immunologic effects of the presence of ligand have been discussed. However, the mechanism of binding has remained elusive. In this study, we show that in solution Bet v 1.0101 is conformationally heterogeneous and cannot be represented by a single structure. NMR relaxation data suggest that structural dynamics are fundamental for ligand access to the protein interior. Complex formation then leads to significant rigidification of the protein along with a compaction of its 3D structure. The data presented herein provide a structural basis for understanding the immunogenic and allergenic potential of ligand binding to Bet v 1 allergens.

Ligand binding modulates the structural dynamics and compactness of the major birch pollen allergen.,Grutsch S, Fuchs JE, Freier R, Kofler S, Bibi M, Asam C, Wallner M, Ferreira F, Brandstetter H, Liedl KR, Tollinger M Biophys J. 2014 Dec 16;107(12):2963-72. doi: 10.1016/j.bpj.2014.10.062. PMID:25517162<ref>PMID:25517162</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4qip" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Betula pendula]]
[[Category: Large Structures]]
[[Category: Brandstetter H]]
[[Category: Freier RA]]
[[Category: Kofler SG]]