View source for 6bkd


==Structure of Hepatitis C Virus Envelope Glycoprotein E2 core from genotype 6a bound to broadly neutralizing antibody AR3D==
<StructureSection load='6bkd' size='340' side='right'caption='[[6bkd]], [[Resolution|resolution]] 3.25&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6bkd]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Recombinant_Hepatitis_C_virus_HK6a/JFH-1 Recombinant Hepatitis C virus HK6a/JFH-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BKD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6BKD 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]] 3.25&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=6bkd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bkd OCA], [https://pdbe.org/6bkd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6bkd RCSB], [https://www.ebi.ac.uk/pdbsum/6bkd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6bkd ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/B9V0E2_9HEPC B9V0E2_9HEPC] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
An effective vaccine to the antigenically diverse hepatitis C virus (HCV) must target conserved immune epitopes. Here, we investigate cross-neutralization of HCV genotypes by broadly neutralizing antibodies (bNAbs) encoded by the relatively abundant human gene family V H 1-69. We have deciphered the molecular requirements for cross-neutralization by this unique class of human antibodies from crystal structures of HCV E2 in complex with bNAbs. An unusually high binding affinity is found for germ line-reverted versions of VH1-69 precursor antibodies, and neutralization breadth is acquired during affinity maturation. Deep sequencing analysis of an HCV-immune B cell repertoire further demonstrates the importance of the V H 1-69 gene family in the generation of HCV bNAbs. This study therefore provides critical insights into immune recognition of HCV with important implications for rational vaccine design.

Genetic and structural insights into broad neutralization of hepatitis C virus by human VH1-69 antibodies.,Tzarum N, Giang E, Kong L, He L, Prentoe J, Augestad E, Hua Y, Castillo S, Lauer GM, Bukh J, Zhu J, Wilson IA, Law M Sci Adv. 2019 Jan 2;5(1):eaav1882. doi: 10.1126/sciadv.aav1882. eCollection 2019 , Jan. PMID:30613781<ref>PMID:30613781</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6bkd" style="background-color:#fffaf0;"></div>

==See Also==
*[[Antibody 3D structures|Antibody 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Recombinant Hepatitis C virus HK6a/JFH-1]]
[[Category: Law M]]
[[Category: Tzarum N]]
[[Category: Wilson IA]]