View source for 7lus


==IgG2 Fc Charge Pair Mutation version 1 (CPMv1)==
<StructureSection load='7lus' size='340' side='right'caption='[[7lus]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7lus]] 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=7LUS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7LUS 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]] 2.45&#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></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=7lus FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7lus OCA], [https://pdbe.org/7lus PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7lus RCSB], [https://www.ebi.ac.uk/pdbsum/7lus PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7lus ProSAT]</span></td></tr>
</table>
== Disease ==
[https://www.uniprot.org/uniprot/IGHG2_HUMAN IGHG2_HUMAN] Recurrent infections associated with rare immunoglobulin isotypes deficiency. 
== Function ==
[https://www.uniprot.org/uniprot/IGHG2_HUMAN IGHG2_HUMAN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Bispecific antibodies (Bispecifics) demonstrate exceptional clinical potential to address some of the most complex diseases. However, Bispecific production in a single cell often requires the correct pairing of multiple polypeptide chains for desired assembly. This is a considerable hurdle that hinders the development of many immunoglobulin G (IgG)-like bispecific formats. Our approach focuses on the rational engineering of charged residues to facilitate the chain pairing of distinct heavy chains (HC). Here, we deploy structure-guided protein design to engineer charge pair mutations (CPMs) placed in the CH3-CH3' interface of the fragment crystallizable (Fc) region of an antibody (Ab) to correctly steer heavy chain pairing. When used in combination with our stable effector functionless 2 (SEFL2.2) technology, we observed high pairing efficiency without significant losses in expression yields. Furthermore, we investigate the relationship between CPMs and the sequence diversity in the parental antibodies, proposing a rational strategy to deploy these engineering technologies.

Next generation Fc scaffold for multispecific antibodies.,Estes B, Sudom A, Gong D, Whittington DA, Li V, Mohr C, Li D, Riley TP, Shi SD, Zhang J, Garces F, Wang Z iScience. 2021 Nov 15;24(12):103447. doi: 10.1016/j.isci.2021.103447. eCollection , 2021 Dec 17. PMID:34877503<ref>PMID:34877503</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7lus" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Garces F]]
[[Category: Sudom A]]
[[Category: Wang Z]]
[[Category: Whittington D]]