HIV interactions with CD4: a continuum of conformations and consequences.
Here, Lee Eiden and Jeffrey Lifson present a model for HIV envelope glycoprotein-CD4 interactions that attempts to reconcile recent, seemingly conflicting, structural, biochemical and biological observations. Central to this model is the involvement of both the CDR2-like and CDR3-like domains of CD4 in the interaction with gp120, leading to a conformational change and dissociation of gp120 from the gp120-gp41 complex.
Eiden
L E
LE
Unit of Molecular and Cellular Neurobiology, National Institute of Mental Health, Bethesda, MD 20892.
Lifson
J D
JD
D001665:Binding Sites; D015704:CD4 Antigens / Q000378:metabolism*; D006678:HIV / Q000378:metabolism*; D015699:HIV Envelope Protein gp120 / Q000378:metabolism*; D015700:HIV Envelope Protein gp41 / Q000378:metabolism; D006801:Humans; D008954:Models, Biological; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation; D013329:Structure-Activity Relationship; D014771:Virion / Q000378:metabolism
D015704:CD4 Antigens; D015699:HIV Envelope Protein gp120; D015700:HIV Envelope Protein gp41