Open AccessStructure-based design of peptides that recognize the CD4 binding domain of HIV-1 gp120
Author(s) -
J. D. Fontenot,
Xin Tan,
David M. Phillips
Publication year - 1998
Publication title -
aids
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.195
H-Index - 216
eISSN - 1473-5571
pISSN - 0269-9370
DOI - 10.1097/00002030-199812000-00002
Subject(s) - epitope , biology , tandem repeat , antibody , gp41 , v3 loop , plasma protein binding , binding site , viral envelope , virology , computational biology , chemistry , human immunodeficiency virus (hiv) , biochemistry , genetics , genome , gene
Envelope protein-specific antiviral peptides, called mucibodies, that can specifically recognize and bind to the surface unit protein gp120 of HIV-1 were designed. The initial mucibody binding target was the V3 loop of HIV-1 gp120. Here, the gp120-CD4 binding domain was chosen as the site of mucibody binding. The CD4 binding domain of gp120 is known to be a conformational epitope and is involved in the earliest events of viral entry into many cells.