View source for 4hk0


==UCA Fab (unbound) from CH65-CH67 Lineage==
<StructureSection load='4hk0' size='340' side='right'caption='[[4hk0]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4hk0]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HK0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HK0 FirstGlance]. <br>
</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=4hk0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hk0 OCA], [https://pdbe.org/4hk0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hk0 RCSB], [https://www.ebi.ac.uk/pdbsum/4hk0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hk0 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q8N355_HUMAN Q8N355_HUMAN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Affinity maturation refines a naive B-cell response by selecting mutations in antibody variable domains that enhance antigen binding. We describe a B-cell lineage expressing broadly neutralizing influenza virus antibodies derived from a subject immunized with the 2007 trivalent vaccine. The lineage comprises three mature antibodies, the unmutated common ancestor, and a common intermediate. Their heavy-chain complementarity determining region inserts into the conserved receptor-binding pocket of influenza HA. We show by analysis of structures, binding kinetics and long time-scale molecular dynamics simulations that antibody evolution in this lineage has rigidified the initially flexible heavy-chain complementarity determining region by two nearly independent pathways and that this preconfiguration accounts for most of the affinity gain. The results advance our understanding of strategies for developing more broadly effective influenza vaccines.

Preconfiguration of the antigen-binding site during affinity maturation of a broadly neutralizing influenza virus antibody.,Schmidt AG, Xu H, Khan AR, O'Donnell T, Khurana S, King LR, Manischewitz J, Golding H, Suphaphiphat P, Carfi A, Settembre EC, Dormitzer PR, Kepler TB, Zhang R, Moody MA, Haynes BF, Liao HX, Shaw DE, Harrison SC Proc Natl Acad Sci U S A. 2012 Nov 21. PMID:23175789<ref>PMID:23175789</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4hk0" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Harrison SC]]
[[Category: Schmidt AG]]