4aka: Difference between revisions
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==IPSE alpha-1, an IgE-binding crystallin== | |||
<StructureSection load='4aka' size='340' side='right'caption='[[4aka]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4aka]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Schistosoma_mansoni Schistosoma mansoni]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AKA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AKA 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=4aka FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4aka OCA], [https://pdbe.org/4aka PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4aka RCSB], [https://www.ebi.ac.uk/pdbsum/4aka PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4aka ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q869D4_SCHMA Q869D4_SCHMA] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
IPSE/alpha-1, the major secretory product of eggs from the parasitic worm Schistosoma mansoni, efficiently triggers basophils to release the immunomodulatory key cytokine interleukin-4. Activation by IPSE/alpha-1 requires the presence of IgE on the basophils, but the detailed molecular mechanism underlying activation is unknown. NMR and crystallographic analysis of IPSEdeltaNLS, a monomeric IPSE/alpha-1 mutant, revealed that IPSE/alpha-1 is a new member of the beta&]gamma]-crystallin superfamily. We demonstrate that this molecule is a general immunoglobulin-binding factor with highest affinity for IgE. NMR binding studies of IPSEdeltaNLS with the 180-kDa molecule IgE identified a large positively charged binding surface that includes a flexible loop, which is unique to the IPSE/alpha-1 crystallin fold. Mutational analysis of amino acids in the binding interface showed that residues contributing to IgE binding are important for IgE-dependent activation of basophils. As IPSE/alpha-1 is unable to cross-link IgE, we propose that this molecule, by taking advantage of its unique IgE-binding crystallin fold, activates basophils by a novel, cross-linking-independent mechanism. | |||
A crystallin fold in the interleukin-4-inducing principle of Schistosoma mansoni eggs (IPSE/alpha-1) mediates IgE binding for antigen-independent basophil activation.,Meyer NH, Mayerhofer H, Tripsianes K, Blindow S, Barths D, Mewes A, Weimar T, Kohli T, Bade S, Madl T, Frey A, Haas H, Mueller-Dieckmann J, Sattler M, Schramm G J Biol Chem. 2015 Jul 10. pii: jbc.M115.675066. PMID:26163514<ref>PMID:26163514</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4aka" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Schistosoma mansoni]] | |||
[[Category: Bade S]] | |||
[[Category: Barths D]] | |||
[[Category: Blindow S]] | |||
[[Category: Frey A]] | |||
[[Category: Haas H]] | |||
[[Category: Madl T]] | |||
[[Category: Mayerhofer H]] | |||
[[Category: Meyer NH]] | |||
[[Category: Mueller-Dieckmann J]] | |||
[[Category: Sattler M]] | |||
[[Category: Scharmm G]] | |||
[[Category: Tripsianes K]] | |||
