View source for 36bb


==Structure of BA.4-S-RBD/Ab#10-M30W-S94M==
<StructureSection load='36bb' size='340' side='right'caption='[[36bb]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[36bb]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Severe_acute_respiratory_syndrome_coronavirus_2 Severe acute respiratory syndrome coronavirus 2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=36BB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=36BB 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=36bb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=36bb OCA], [https://pdbe.org/36bb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=36bb RCSB], [https://www.ebi.ac.uk/pdbsum/36bb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=36bb ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
The ongoing evolution of SARS-CoV-2, particularly the emergence of Omicron subvariants, compromised the effectiveness of many therapeutic antibodies. In this study, we employed a structure-guided computational design strategy to systematically optimize the COV2-2196 antibody for improved neutralization of Omicron variants. Through iterative rounds of computational design and experimental validation, we identified key paratope mutations that restored and enhanced antibody binding and neutralization potency against resistant viral strains. Cryo-EM structural analysis revealed the molecular basis for these improvements, highlighting how targeted modifications can accommodate epitope changes introduced by viral evolution. Our approach demonstrates that effective antibody optimization can be achieved using accessible computational resources, providing a practical framework for rapid therapeutic development. These findings underscore the potential of structure-based design to address challenges posed by viral antigenic drift and support the development of broadly effective antibody therapeutics for emerging infectious diseases.

Structure-Guided Design of Therapeutic Antibodies Targeting SARS-CoV-2 Omicron Variants.,Pallesen J, Du J, Wu Y, Ghosh S, Bayruns K, Sadeesh R, Weiner D Res Sq [Preprint]. 2026 Jun 24:rs.3.rs-9917568. doi: 10.21203/rs.3.rs-9917568/v1. PMID:42396495<ref>PMID:42396495</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 36bb" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Severe acute respiratory syndrome coronavirus 2]]
[[Category: Du J]]
[[Category: Pallesen J]]