Your browser doesn't support javascript.
loading
Unexpected structure for the N-terminal domain of hepatitis C virus envelope glycoprotein E1.
El Omari, Kamel; Iourin, Oleg; Kadlec, Jan; Sutton, Geoff; Harlos, Karl; Grimes, Jonathan M; Stuart, David I.
Afiliación
  • El Omari K; 1] Division of Structural Biology, The Wellcome Trust Centre for Human Genetics, University of Oxford, Headington, Oxford OX3 7BN, UK [2].
  • Iourin O; 1] Division of Structural Biology, The Wellcome Trust Centre for Human Genetics, University of Oxford, Headington, Oxford OX3 7BN, UK [2].
  • Kadlec J; 1] Division of Structural Biology, The Wellcome Trust Centre for Human Genetics, University of Oxford, Headington, Oxford OX3 7BN, UK [2].
  • Sutton G; Division of Structural Biology, The Wellcome Trust Centre for Human Genetics, University of Oxford, Headington, Oxford OX3 7BN, UK.
  • Harlos K; Division of Structural Biology, The Wellcome Trust Centre for Human Genetics, University of Oxford, Headington, Oxford OX3 7BN, UK.
  • Grimes JM; 1] Division of Structural Biology, The Wellcome Trust Centre for Human Genetics, University of Oxford, Headington, Oxford OX3 7BN, UK [2] Diamond Light Source Limited, Harwell Science and Innovation Campus, Didcot OX11 0DE, UK.
  • Stuart DI; 1] Division of Structural Biology, The Wellcome Trust Centre for Human Genetics, University of Oxford, Headington, Oxford OX3 7BN, UK [2] Diamond Light Source Limited, Harwell Science and Innovation Campus, Didcot OX11 0DE, UK.
Nat Commun ; 5: 4874, 2014 Sep 16.
Article en En | MEDLINE | ID: mdl-25224686
ABSTRACT
Hepatitis C virus (HCV) infection remains a major health problem worldwide. HCV entry into host cells and membrane fusion are achieved by two envelope glycoproteins, E1 and E2. We report here the 3.5-Å resolution crystal structure of the N-terminal domain of the HCV E1 ectodomain, which reveals a complex network of covalently linked intertwined homodimers that do not harbour the expected truncated class II fusion protein fold.
Asunto(s)
Texto completo
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Base de datos: MEDLINE Asunto principal: Proteínas del Envoltorio Viral / Hepacivirus Idioma: En Revista: Nat Commun Asunto de la revista: BIOLOGIA / CIENCIA Año: 2014 Tipo del documento: Article
Texto completo
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Base de datos: MEDLINE Asunto principal: Proteínas del Envoltorio Viral / Hepacivirus Idioma: En Revista: Nat Commun Asunto de la revista: BIOLOGIA / CIENCIA Año: 2014 Tipo del documento: Article