| Literature DB >> 22973046 |
Leopold Kong1, Erick Giang, Travis Nieusma, Justin B Robbins, Marc C Deller, Robyn L Stanfield, Ian A Wilson, Mansun Law.
Abstract
We have determined the crystal structure of the broadly neutralizing antibody (bnAb) AP33, bound to a peptide corresponding to hepatitis C virus (HCV) E2 envelope glycoprotein antigenic site 412 to 423. Comparison with bnAb HCV1 bound to the same epitope reveals a different angle of approach to the antigen by bnAb AP33 and slight variation in its β-hairpin conformation of the epitope. These structures establish two different modes of binding to E2 that antibodies adopt to neutralize diverse HCV.Entities:
Mesh:
Substances:
Year: 2012 PMID: 22973046 PMCID: PMC3497658 DOI: 10.1128/JVI.01939-12
Source DB: PubMed Journal: J Virol ISSN: 0022-538X Impact factor: 5.103