View source for 5vjq


==Complex between HyHEL10 Fab fragment heavy chain mutant (I29F, S52T, Y53F) and Pekin duck egg lysozyme isoform I (DEL-I)==
<StructureSection load='5vjq' size='340' side='right'caption='[[5vjq]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5vjq]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Anas_platyrhynchos Anas platyrhynchos] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VJQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5VJQ 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]] 1.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=5vjq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vjq OCA], [https://pdbe.org/5vjq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5vjq RCSB], [https://www.ebi.ac.uk/pdbsum/5vjq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5vjq ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Antibodies have the specificity to differentiate foreign antigens that mimic self antigens, but it remains unclear how such specificity is acquired. In a mouse model, we generated B cells displaying an antibody that cross-reacts with two related protein antigens expressed on self versus foreign cells. B cell anergy was imposed by self antigen but reversed upon challenge with high-density foreign antigen, leading to germinal center recruitment and antibody gene hypermutation. Single-cell analysis detected rapid selection for mutations that decrease self affinity and slower selection for epistatic mutations that specifically increase foreign affinity. Crystal structures revealed that these mutations exploited subtle topological differences to achieve 5000-fold preferential binding to foreign over self epitopes. Resolution of antigenic mimicry drove the optimal affinity maturation trajectory, highlighting the value of retaining self-reactive clones as substrates for protective antibody responses.

Germinal center antibody mutation trajectories are determined by rapid self/foreign discrimination.,Burnett DL, Langley DB, Schofield P, Hermes JR, Chan TD, Jackson J, Bourne K, Reed JH, Patterson K, Porebski BT, Brink R, Christ D, Goodnow CC Science. 2018 Apr 13;360(6385):223-226. doi: 10.1126/science.aao3859. PMID:29650674<ref>PMID:29650674</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5vjq" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Anas platyrhynchos]]
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Christ D]]
[[Category: Langley DB]]