4bk6
From Proteopedia
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| - | {{STRUCTURE_4bk6| PDB=4bk6 | SCENE= }} | ||
| - | ===Crystal Structure of a dimeric variant of Bet v 1=== | ||
| - | {{ABSTRACT_PUBMED_24253036}} | ||
| - | == | + | ==Crystal Structure of a dimeric variant of Bet v 1== |
| - | [[http://www.uniprot.org/uniprot/BEV1A_BETPN BEV1A_BETPN | + | <StructureSection load='4bk6' size='340' side='right'caption='[[4bk6]], [[Resolution|resolution]] 1.63Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4bk6]] is a 2 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=4BK6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BK6 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]] 1.63Å</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=4bk6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bk6 OCA], [https://pdbe.org/4bk6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bk6 RCSB], [https://www.ebi.ac.uk/pdbsum/4bk6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bk6 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 == | ||
| + | Many allergens share several biophysical characteristics, including the capability to undergo oligomerisation. The dimerization mechanism in Bet v 1 and its allergenic properties are so far poorly understood. Here, we report crystal structures of dimeric Bet v 1, revealing a non-canonical incorporation of cysteine at position 5 instead of genetically encoded tyrosine. Cysteine polysulfide bridging stabilized different dimeric assemblies, depending on the polysulfide linker length. These dimers represent quaternary arrangements that are frequently observed in related proteins, reflecting their prevalence in unmodified Bet v 1. These conclusions were corroborated by characteristic immunologic properties of monomeric and dimeric allergen variants. Hereby, residue 5 could be identified as an allergenic hot spot in Bet v 1. The presented results refine fundamental principles in protein chemistry, and emphasize the importance of protein modifications in understanding the molecular basis of allergenicity. | ||
| - | + | Stabilization of the dimeric birch pollen allergen Bet v 1 impacts its immunological properties.,Kofler S, Ackaert C, Samonig M, Asam C, Briza P, Horejs-Hoeck J, Cabrele C, Ferreira F, Duschl A, Huber C, Brandstetter H J Biol Chem. 2013 Nov 19. PMID:24253036<ref>PMID:24253036</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | < | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 4bk6" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Betula pendula]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Brandstetter H]] | ||
| + | [[Category: Kofler SG]] | ||
Current revision
Crystal Structure of a dimeric variant of Bet v 1
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