View source for 6wib


==Next generation monomeric IgG4 Fc==
<StructureSection load='6wib' size='340' side='right'caption='[[6wib]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6wib]] is a 1 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=6WIB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6WIB 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]] 2.55&#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=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=6wib FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6wib OCA], [https://pdbe.org/6wib PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6wib RCSB], [https://www.ebi.ac.uk/pdbsum/6wib PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6wib ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/IGHG4_HUMAN IGHG4_HUMAN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
In a biologic therapeutic landscape that requires versatility in targeting specificity, valency and half-life modulation, the monomeric Fc fusion platform holds exciting potential for the creation of a class of monovalent protein therapeutics that includes fusion proteins and bispecific targeting molecules. Here we report a structure-guided approach to engineer monomeric Fc molecules to adapt multiple versions of half-life extension modifications. Co-crystal structures of these monomeric Fc variants with Fc neonatal receptor (FcRn) shed light into the binding interactions that could serve as a guide for engineering the half-life of antibody Fc fragments. These engineered monomeric Fc molecules also enabled the generation of a novel monovalent bispecific molecular design, which translated the FcRn binding enhancement to improvement of in vivo serum half-life.

In vivo pharmacokinetic enhancement of monomeric Fc and monovalent bispecific designs through structural guidance.,Shan L, Dyk NV, Haskins N, Cook KM, Rosenthal KL, Mazor R, Dragulin-Otto S, Jiang Y, Wu H, Dall'Acqua WF, Borrok MJ, Damschroder MM, Oganesyan V Commun Biol. 2021 Sep 8;4(1):1048. doi: 10.1038/s42003-021-02565-5. PMID:34497355<ref>PMID:34497355</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6wib" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Dall'Acqua W]]
[[Category: Oganesyan VY]]
[[Category: Shan L]]
[[Category: Van Dyk N]]