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Structure of hepatitis C virus envelope glycoprotein E2 antigenic site 412 to 423 in complex with antibody AP33.
Kong, Leopold; Giang, Erick; Nieusma, Travis; Robbins, Justin B; Deller, Marc C; Stanfield, Robyn L; Wilson, Ian A; Law, Mansun.
Afiliação
  • Kong L; Department of Molecular Biology, The Scripps Research Institute, La Jolla, California, USA.
J Virol ; 86(23): 13085-8, 2012 Dec.
Article em En | MEDLINE | ID: mdl-22973046
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 ß-hairpin conformation of the epitope. These structures establish two different modes of binding to E2 that antibodies adopt to neutralize diverse HCV.
Assuntos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Conformação Proteica / Modelos Moleculares / Proteínas do Envelope Viral / Hepacivirus / Anticorpos Neutralizantes Idioma: En Ano de publicação: 2012 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Conformação Proteica / Modelos Moleculares / Proteínas do Envelope Viral / Hepacivirus / Anticorpos Neutralizantes Idioma: En Ano de publicação: 2012 Tipo de documento: Article