Circular dichroism study on the secondary structural change induced by complex formation of a peptide derived from a CD4 binding site of HIV-1 envelope glycoprotein gp120 and a peptide from the N-terminal domain of CD4

1996 ◽  
Vol 3 (5) ◽  
pp. 293-300
Author(s):  
Ding-Kwo Chang ◽  
Shu-Fang Cheng
Keyword(s):  
Structural Change ◽  
Complex Formation ◽  
Binding Site ◽  
Envelope Glycoprotein ◽  
Terminal Domain ◽  
Envelope Glycoprotein Gp120 ◽  
Cd4 Binding Site ◽  
Glycoprotein Gp120 ◽  
Secondary Structural Change ◽  
Hiv 1

scholarly journals In vivo alteration of humoral responses to HIV-1 envelope glycoprotein gp120 by antibodies to the CD4-binding site of gp120

Virology ◽  
2008 ◽  
Vol 372 (2) ◽  
pp. 409-420 ◽  
Author(s):  
Maria Luisa Visciano ◽  
Michael Tuen ◽  
Miroslaw K. Gorny ◽  
Catarina E. Hioe
Keyword(s):  
Binding Site ◽  
Envelope Glycoprotein ◽  
Envelope Glycoprotein Gp120 ◽  
Cd4 Binding Site ◽  
Glycoprotein Gp120 ◽  
Humoral Responses ◽  
Hiv 1

scholarly journals Heparan Sulfate Targets the HIV-1 Envelope Glycoprotein gp120 Coreceptor Binding Site

2005 ◽  
Vol 280 (22) ◽  
pp. 21353-21357 ◽  
Author(s):  
Romain R. Vivès ◽  
Anne Imberty ◽  
Quentin J. Sattentau ◽  
Hugues Lortat-Jacob
Keyword(s):  
Heparan Sulfate ◽  
Binding Site ◽  
Envelope Glycoprotein ◽  
Envelope Glycoprotein Gp120 ◽  
Coreceptor Binding ◽  
Glycoprotein Gp120 ◽  
Hiv 1 ◽  
Coreceptor Binding Site

scholarly journals Targeted deletion in the β20–β21 loop of HIV envelope glycoprotein gp120 exposes the CD4 binding site for antibody binding

Virology ◽  
2008 ◽  
Vol 377 (2) ◽  
pp. 330-338 ◽  
Author(s):  
Ira Berkower ◽  
Chiraag Patel ◽  
Yisheng Ni ◽  
Konstantin Virnik ◽  
Zhexin Xiang ◽  
...  
Keyword(s):  
Binding Site ◽  
Envelope Glycoprotein ◽  
Antibody Binding ◽  
Targeted Deletion ◽  
Envelope Glycoprotein Gp120 ◽  
Cd4 Binding Site ◽  
Glycoprotein Gp120 ◽  
Hiv Envelope

scholarly journals Peptides presenting the binding site of human CD4 for the HIV-1 envelope glycoprotein gp120

2012 ◽  
Vol 8 ◽  
pp. 1858-1866 ◽  
Author(s):  
Julia Meier ◽  
Kristin Kassler ◽  
Heinrich Sticht ◽  
Jutta Eichler
Keyword(s):  
Amino Acids ◽  
Binding Site ◽  
Envelope Glycoprotein ◽  
Conformational Stability ◽  
Cellular Receptor ◽  
Binding Assays ◽  
Glycoprotein Gp120 ◽  
Dynamics Simulations ◽  
Key Residues ◽  
Hiv 1

Based on the structure of the HIV-1 glycoprotein gp120 in complex with its cellular receptor CD4, we have designed and synthesized peptides that mimic the binding site of CD4 for gp120. The ability of these peptides to bind to gp120 can be strongly enhanced by increasing their conformational stability through cyclization, as evidenced by binding assays, as well as through molecular-dynamics simulations of peptide–gp120 complexes. The specificity of the peptide–gp120 interaction was demonstrated by using peptide variants, in which key residues for the interaction with gp120 were replaced by alanine or D-amino acids.

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