Crystal structure of the neutralizing Llama V(HH) D7 and its mode of HIV-1 gp120 interaction.
HIV-1 entry into host cells is mediated by the sequential binding of the envelope glycoprotein gp120 to CD4 and a chemokine receptor. Antibodies binding to epitopes overlapping the CD4-binding site on gp120 are potent inhibitors of HIV entry, such as the llama heavy chain antibody fragment V(HH) D7,...
Guardado en:
Autores principales: | Andreas Hinz, David Lutje Hulsik, Anna Forsman, Willie Wee-Lee Koh, Hassan Belrhali, Andrea Gorlani, Hans de Haard, Robin A Weiss, Theo Verrips, Winfried Weissenhorn |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Public Library of Science (PLoS)
2010
|
Materias: | |
Acceso en línea: | https://doaj.org/article/cc4438b984d14872b7496273180a0aa0 |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
Crystal structure and size-dependent neutralization properties of HK20, a human monoclonal antibody binding to the highly conserved heptad repeat 1 of gp41.
por: Charles Sabin, et al.
Publicado: (2010) -
Geospatial HIV-1 subtype C gp120 sequence diversity and its predicted impact on broadly neutralizing antibody sensitivity.
por: Jyoti Sutar, et al.
Publicado: (2021) -
Identification and characterization of a broadly cross-reactive HIV-1 human monoclonal antibody that binds to both gp120 and gp41.
por: Mei-Yun Zhang, et al.
Publicado: (2012) -
Glycoform and net charge heterogeneity in gp120 immunogens used in HIV vaccine trials.
por: Bin Yu, et al.
Publicado: (2012) -
Atomic force microscopy fishing and mass spectrometry identification of gp120 on immobilized aptamers
por: Ivanov YD, et al.
Publicado: (2014)