View source for 8sal


==CryoEM structure of VRC01-CH848.0358.80==
<StructureSection load='8sal' size='340' side='right'caption='[[8sal]], [[Resolution|resolution]] 4.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8sal]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/HIV-1_06TG.HT008 HIV-1 06TG.HT008] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8SAL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8SAL 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]] 4.9&#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=8sal FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8sal OCA], [https://pdbe.org/8sal PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8sal RCSB], [https://www.ebi.ac.uk/pdbsum/8sal PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8sal ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Antibody affinity maturation enables adaptive immune responses to a wide range of pathogens. In some individuals broadly neutralizing antibodies develop to recognize rapidly mutating pathogens with extensive sequence diversity. Vaccine design for pathogens such as HIV-1 and influenza has therefore focused on recapitulating the natural affinity maturation process. Here, we determine structures of antibodies in complex with HIV-1 Envelope for all observed members and ancestral states of the broadly neutralizing HIV-1 V3-glycan targeting DH270 antibody clonal B cell lineage. These structures track the development of neutralization breadth from the unmutated common ancestor and define affinity maturation at high spatial resolution. By elucidating contacts mediated by key mutations at different stages of antibody development we identified sites on the epitope-paratope interface that are the focus of affinity optimization. Thus, our results identify bottlenecks on the path to natural affinity maturation and reveal solutions for these that will inform immunogen design aimed at eliciting a broadly neutralizing immune response by vaccination.

Structural basis for breadth development in the HIV-1 V3-glycan targeting DH270 antibody clonal lineage.,Henderson R, Zhou Y, Stalls V, Wiehe K, Saunders KO, Wagh K, Anasti K, Barr M, Parks R, Alam SM, Korber B, Haynes BF, Bartesaghi A, Acharya P Nat Commun. 2023 May 15;14(1):2782. doi: 10.1038/s41467-023-38108-1. PMID:37188681<ref>PMID:37188681</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8sal" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: HIV-1 06TG HT008]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Acharya P]]
[[Category: Bartesaghi B]]
[[Category: Henderson R]]
[[Category: Stalls V]]
[[Category: Zhou Y]]