2xa8: Difference between revisions

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-'''Unreleased structure'''
-The entry 2xa8 is ON HOLD  until Mar 30 2012
+==Crystal structure of the Fab domain of omalizumab at 2.41A==
+<StructureSection load='2xa8' size='340' side='right'caption='[[2xa8]], [[Resolution|resolution]] 2.42&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2xa8]] is a 2 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=2XA8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XA8 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]] 2.42&#8491;</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=2xa8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xa8 OCA], [https://pdbe.org/2xa8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xa8 RCSB], [https://www.ebi.ac.uk/pdbsum/2xa8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xa8 ProSAT]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Omalizumab, an anti-IgE antibody, used to treat severe allergic asthma and chronic idiopathic urticaria, binds to IgE in blood or membrane-bound on B lymphocytes but not to IgE bound to its high (FcepsilonRI) or low (CD23) affinity receptor. Mutagenesis studies indicate overlapping FcepsilonRI and omalizumab-binding sites in the Cepsilon3 domain, but crystallographic studies show FcepsilonRI and CD23-binding sites that are far apart, so how can omalizumab block IgE from binding both receptors? We report a 2.42-A omalizumab-Fab structure, a docked IgE-Fc/omalizumab-Fab structure consistent with available experimental data, and the free energy contributions of IgE residues to binding omalizumab, CD23, and FcepsilonRI. These results provide a structural and physical basis as to why omalizumab cannot bind receptor-bound IgE and why omalizumab-bound IgE cannot bind to CD23/FcepsilonRI. They reveal the key IgE residues and their roles in binding omalizumab, CD23, and FcepsilonRI.
-Authors: Huang, C.H., Hung, F.H.A., Lim, C., Chang, T.W., Ma, C.
+Structural and Physical Basis for Anti-IgE Therapy.,Wright JD, Chu HM, Huang CH, Ma C, Chang TW, Lim C Sci Rep. 2015 Jun 26;5:11581. doi: 10.1038/srep11581. PMID:26113483<ref>PMID:26113483</ref>
-Description: Crystal structure of the Fab domain of omalizumab at 2.41A
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Sep  1 09:28:21 2010''
+<div class="pdbe-citations 2xa8" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Chang TW]]
+[[Category: Huang CH]]
+[[Category: Hung FHA]]
+[[Category: Lim C]]
+[[Category: Ma C]]