4q0x: Difference between revisions

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 <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4q0x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q0x OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4q0x RCSB], [http://www.ebi.ac.uk/pdbsum/4q0x PDBsum]</span></td></tr>
 <table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The X-ray crystal structure of epitope II on the E2 protein of hepatitis C virus, in complex with nonneutralizing antibody mAb#12, has been solved at 2.90-A resolution. The spatial arrangement of the essential components of epitope II (ie, the C-terminal alpha-helix and the N-terminal loop) was found to deviate significantly from that observed in those corresponding complexes with neutralizing antibodies. The distinct conformations are mediated largely by the flexibility of a highly conserved glycine residue that connects these components. Thus, it is the particular tertiary structure of epitope II, which is presented in a spatial and temporal manner, that determines the specificity of antibody recognition and, consequently, the outcome of neutralization or nonneutralization.
+Discrete conformations of epitope II on the hepatitis C virus E2 protein for antibody-mediated neutralization and nonneutralization.,Deng L, Ma L, Virata-Theimer ML, Zhong L, Yan H, Zhao Z, Struble E, Feinstone S, Alter H, Zhang P Proc Natl Acad Sci U S A. 2014 Jul 7. pii: 201411317. PMID:25002515<ref>PMID:25002515</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+== References ==
+<references/>
 __TOC__
 </StructureSection>