4q0x

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.