Structural basis of HIV-1 neutralization by affinity matured Fabs directed against the internal trimeric coiled-coil of gp41

The conserved internal trimeric coiled-coil of the N-heptad repeat (N-HR) of HIV-1 gp41 is transiently exposed during the fusion process by forming a pre-hairpin intermediate, thus representing an attractive target for the design of fusion inhibitors and neutralizing antibodies. In previous studies...

Ausführliche Beschreibung

Gespeichert in:

Bibliographische Detailangaben
Veröffentlicht in:	PLoS Patho 2010-11, Vol.6 (11), p.e1001182
Hauptverfasser:	Gustchina, Elena, Li, Mi, Louis, John M, Anderson, D Eric, Lloyd, John, Frisch, Christian, Bewley, Carole A, Gustchina, Alla, Wlodawer, Alexander, Clore, G Marius
Format:	Artikel
Sprache:	eng
Schlagworte:	AFFINITY Amino Acid Sequence ANTIBODIES Antibodies, Monoclonal - immunology Antibodies, Monoclonal - metabolism Antibodies, Neutralizing - immunology Antibodies, Neutralizing - metabolism antibody libraries Cancer CD4 antigen Chemokines Complementarity Conformation CONVERGENCE CRYSTAL STRUCTURE Crystallography, X-Ray DESIGN DIVERSIFICATION Envelopes Fab Glycoprotein gp120 glycoprotein gp41 Glycoproteins HIV (Viruses) HIV Antibodies - immunology HIV Antibodies - metabolism HIV Envelope Protein gp41 - chemistry HIV Envelope Protein gp41 - immunology HIV Envelope Protein gp41 - metabolism HIV-1 - immunology HIV-1 - metabolism Human immunodeficiency virus 1 Humans Infection Infectious Diseases/HIV Infection and AIDS Library collections MATERIALS SCIENCE Medical research Membrane fusion Models, Molecular Molecular Sequence Data Monoclonal antibodies Neutralization Tests Panning Pathogens Physiological aspects Protein Conformation Sequence Homology, Amino Acid SIMULATION TARGETS VIRUSES
Online-Zugang:	Volltext
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!

Schreiben Sie den ersten Kommentar!