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Updated: Aug 2, 2026
10:50
Assessment of Immunologically Relevant Dynamic Tertiary Structural Features of the HIV-1 V3 Loop Crown R2 Sequence by ab initio Folding
Published on: September 16, 2010
HIV interactions with CD4: a continuum of conformations and consequences
1Unit of Molecular and Cellular Neurobiology, National Institute of Mental Health, Bethesda, MD 20892.
Immunology Today
|June 1, 1992
Summary
This study proposes a new model for HIV envelope glycoprotein (gp120) and CD4 receptor interactions. The model explains how CD4 domains binding to gp120 cause conformational changes, crucial for viral entry.
Area of Science:
- Virology
- Structural Biology
- Immunology
Background:
- HIV entry relies on interactions between the viral envelope glycoprotein (gp120) and the host cell receptor CD4.
- Conflicting structural, biochemical, and biological data have complicated the understanding of these interactions.
Purpose of the Study:
- To present a unifying model for HIV envelope glycoprotein-CD4 interactions.
- To reconcile disparate observations regarding the binding of gp120 to CD4.
Main Methods:
- The study presents a theoretical model based on integrating existing structural, biochemical, and biological data.
- No new experimental data were generated; the focus is on model synthesis.
Main Results:
- The proposed model highlights the critical role of both CDR2-like and CDR3-like domains of CD4 in binding to gp120.
- This interaction induces a conformational change in gp120, facilitating its dissociation from the gp120-gp41 complex.
Conclusions:
- The model provides a framework for understanding the molecular mechanisms of HIV-CD4 binding.
- This understanding may inform the development of novel therapeutic strategies targeting HIV entry.
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