View source for 6uqr


==Complex of IgE and Ligelizumab==
<StructureSection load='6uqr' size='340' side='right'caption='[[6uqr]], [[Resolution|resolution]] 3.65&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6uqr]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6UQR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6UQR 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]] 3.6502912&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=6uqr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6uqr OCA], [https://pdbe.org/6uqr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6uqr RCSB], [https://www.ebi.ac.uk/pdbsum/6uqr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6uqr ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/IGHE_HUMAN IGHE_HUMAN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Targeting of immunoglobulin E (IgE) represents an interesting approach for the treatment of allergic disorders. A high-affinity monoclonal anti-IgE antibody, ligelizumab, has recently been developed to overcome some of the limitations associated with the clinical use of the therapeutic anti-IgE antibody, omalizumab. Here, we determine the molecular binding profile and functional modes-of-action of ligelizumab. We solve the crystal structure of ligelizumab bound to IgE, and report epitope differences between ligelizumab and omalizumab that contribute to their qualitatively distinct IgE-receptor inhibition profiles. While ligelizumab shows superior inhibition of IgE binding to FcepsilonRI, basophil activation, IgE production by B cells and passive systemic anaphylaxis in an in vivo mouse model, ligelizumab is less potent in inhibiting IgE:CD23 interactions than omalizumab. Our data thus provide a structural and mechanistic foundation for understanding the efficient suppression of FcepsilonRI-dependent allergic reactions by ligelizumab in vitro as well as in vivo.

The mechanistic and functional profile of the therapeutic anti-IgE antibody ligelizumab differs from omalizumab.,Gasser P, Tarchevskaya SS, Guntern P, Brigger D, Ruppli R, Zbaren N, Kleinboelting S, Heusser C, Jardetzky TS, Eggel A Nat Commun. 2020 Jan 8;11(1):165. doi: 10.1038/s41467-019-13815-w. PMID:31913280<ref>PMID:31913280</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6uqr" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Jardetzky TS]]
[[Category: Kleinboelting S]]
[[Category: Tarchevskaya SS]]