7lxk
From Proteopedia
(Difference between revisions)
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<StructureSection load='7lxk' size='340' side='right'caption='[[7lxk]]' scene=''> | <StructureSection load='7lxk' size='340' side='right'caption='[[7lxk]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>Full | + | <table><tr><td colspan='2'>[[7lxk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arachis_hypogaea Arachis hypogaea]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7LXK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7LXK FirstGlance]. <br> |
</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=7lxk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7lxk OCA], [https://pdbe.org/7lxk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7lxk RCSB], [https://www.ebi.ac.uk/pdbsum/7lxk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7lxk ProSAT]</span></td></tr> | </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=7lxk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7lxk OCA], [https://pdbe.org/7lxk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7lxk RCSB], [https://www.ebi.ac.uk/pdbsum/7lxk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7lxk ProSAT]</span></td></tr> | ||
</table> | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/ALL12_ARAHY ALL12_ARAHY] | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Vicilin-buried peptides (VBPs) from edible plants are derived from the N-terminal leader sequences (LSs) of seed storage proteins. VBPs are defined by a common alpha-hairpin fold mediated by conserved CxxxCx(10-14)CxxxC motifs. Here, peanut and walnut VBPs were characterized as potential mediators of both peanut/walnut allergenicity and cross-reactivity despite their low ( approximately 17%) sequence identity. The structures of one peanut (AH1.1) and 3 walnut (JR2.1, JR2.2, JR2.3) VBPs were solved using solution NMR, revealing similar alpha-hairpin structures stabilized by disulfide bonds with high levels of surface similarity. Peptide microarrays identified several peptide sequences primarily on AH1.1 and JR2.1, which were recognized by peanut-, walnut-, and dual-allergic patient IgE, establishing these peanut and walnut VBPs as potential mediators of allergenicity and cross-reactivity. JR2.2 and JR2.3 displayed extreme resilience against endosomal digestion, potentially hindering epitope generation and likely contributing to their reduced allergic potential. | ||
+ | |||
+ | Structure, Immunogenicity, and IgE Cross-Reactivity among Walnut and Peanut Vicilin-Buried Peptides.,Foo ACY, Nesbit JB, Gipson SAY, Cheng H, Bushel P, DeRose EF, Schein CH, Teuber SS, Hurlburt BK, Maleki SJ, Mueller GA J Agric Food Chem. 2022 Feb 9. doi: 10.1021/acs.jafc.1c07225. PMID:35139305<ref>PMID:35139305</ref> | ||
+ | |||
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 7lxk" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
+ | [[Category: Arachis hypogaea]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: London R]] | [[Category: London R]] | ||
[[Category: Mueller G]] | [[Category: Mueller G]] |
Revision as of 07:32, 22 March 2023
Ara h 1 leader sequence, Ara h 1.0101 (25-83) A25G
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