View source for 5ubx


==Crystal structure of a mutant mIgG2b Fc heterodimer in complex with Protein A peptide analog Z34C==
<StructureSection load='5ubx' size='340' side='right'caption='[[5ubx]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5ubx]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UBX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5UBX 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]] 2.7&#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=5ubx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ubx OCA], [https://pdbe.org/5ubx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ubx RCSB], [https://www.ebi.ac.uk/pdbsum/5ubx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ubx ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/IGG2B_MOUSE IGG2B_MOUSE] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The increased number of bispecific antibodies (BsAb) under therapeutic development has resulted in a need for mouse surrogate BsAbs. Here, we describe a one-step method for generating highly pure mouse BsAbs suitable for in vitro and in vivo studies. We identify two mutations in the mouse IgG2a and IgG2b Fc region: one that eliminates protein A binding and one that enhances protein A binding by 8-fold. We show that BsAbs harboring these mutations can be purified from the residual parental monoclonal antibodies in one step using protein A affinity chromatography. The structural basis for the effects of these mutations was analyzed by X-ray crystallography. While the mutation that disrupted protein A binding also inhibited FcRn interaction, a bispecific mutant in which one subunit retained the ability to bind protein A could still interact with FcRn. Pharmacokinetic analysis of the serum half-lives of the mutants showed that the mutant BsAb had a serum half-life comparable to a wild-type Ab. The results describe a rapid method for generating panels of mouse BsAbs that could be used in mouse studies.

Modulation of protein A binding allows single-step purification of mouse bispecific antibodies that retain FcRn binding.,Zwolak A, Armstrong AA, Tam SH, Pardinas JR, Goulet DR, Zheng S, Brosnan K, Emmell E, Luo J, Gilliland GL, Chiu ML MAbs. 2017 Sep 12:0. doi: 10.1080/19420862.2017.1375639. PMID:28898162<ref>PMID:28898162</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5ubx" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Staphylococcus aureus]]
[[Category: Armstrong AA]]
[[Category: Gilliland GL]]
[[Category: Zwolak A]]