View source for 8w5o


==Cryo-EM structure of Qb-Ab31==
<StructureSection load='8w5o' size='340' side='right'caption='[[8w5o]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8w5o]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_phage_Qbeta Escherichia phage Qbeta] 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=8W5O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8W5O FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.6&#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=8w5o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8w5o OCA], [https://pdbe.org/8w5o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8w5o RCSB], [https://www.ebi.ac.uk/pdbsum/8w5o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8w5o ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A1_BPQBE A1_BPQBE] Minor capsid protein.<ref>PMID:21805520</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The germinal center (GC) sets an environment where antigen-specific B cells are compelled to continuously increase their affinity to compete for the antigen and obtain Tfh help for survival and propagation. Previous studies indicated that low-affinity B cells are disadvantaged in the presence of high-affinity ones, suggesting that competition may lead to the elimination of low-affinity B cells and their descendants. However, using a multivalent virus-mimicking antigen, our study demonstrates that low-affinity B cells not only successfully participate in GC responses alongside high-affinity B cells but also undergo accelerated affinity maturation under the more stringent competition. Furthermore, our cryo-electron-microscopy-based structural analysis reveals that both low-affinity and high-affinity B cells compete for the same antigenic epitope. Although the applicability of this idealized GC competition to true pathogen-induced responses remains uncertain, this change in perspective on the role of competition in low-affinity B cell evolution provides valuable insights for vaccine development.

Competition propels, rather than limits, the success of low-affinity B cells in the germinal center response.,Li R, Bao K, Liu C, Ma X, Hua Z, Zhu P, Hou B Cell Rep. 2025 Feb 15;44(2):115334. doi: 10.1016/j.celrep.2025.115334. PMID:39955776<ref>PMID:39955776</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8w5o" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia phage Qbeta]]
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Bao KY]]
[[Category: Hou BD]]
[[Category: Hua ZL]]
[[Category: Li RH]]
[[Category: Zhu P]]