Oligomeric and Conformational Properties of a Proteolytically Mature, Disulfide-Stabilized Human Immunodeficiency Virus Type 1 gp140 Envelope Glycoprotein

We describe the further properties of a protein, designated SOS gp140, wherein the association of the gp120 and gp41 subunits of the human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein is stabilized by an intersubunit disulfide bond. HIV-1(JR-FL) SOS gp140, proteolytically uncleaved gp...

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Detalhes bibliográficos
Main Authors: Schülke, Norbert, Vesanen, Mika S., Sanders, Rogier W., Zhu, Ping, Lu, Min, Anselma, Deborah J., Villa, Anthony R., Parren, Paul W. H. I., Binley, James M., Roux, Kenneth H., Maddon, Paul J., Moore, John P., Olson, William C.
Formato: Artigo
Idioma:Inglês
Publicado em: American Society for Microbiology 2002
Assuntos:
Structure and Assembly
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC136400/
https://ncbi.nlm.nih.gov/pubmed/12097589
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1128/JVI.76.15.7760-7776.2002
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