A conserved HIV gp120 glycoprotein structure involved in chemokine receptor binding.

Article Details

Citation

Rizzuto CD, Wyatt R, Hernandez-Ramos N, Sun Y, Kwong PD, Hendrickson WA, Sodroski J

A conserved HIV gp120 glycoprotein structure involved in chemokine receptor binding.

Science. 1998 Jun 19;280(5371):1949-53.

PubMed ID
9632396 [ View in PubMed
]
Abstract

The entry of primate immunodeficiency viruses into target cells depends on a sequential interaction of the gp120 envelope glycoprotein with the cellular receptors, CD4 and members of the chemokine receptor family. The gp120 third variable (V3) loop has been implicated in chemokine receptor binding, but the use of the CCR5 chemokine receptor by diverse primate immunodeficiency viruses suggests the involvement of an additional, conserved gp120 element. Through the use of gp120 mutants, a highly conserved gp120 structure was shown to be critical for CCR5 binding. This structure is located adjacent to the V3 loop and contains neutralization epitopes induced by CD4 binding. This conserved element may be a useful target for pharmacologic or prophylactic intervention in human immunodeficiency virus (HIV) infections.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
C-C chemokine receptor type 5P51681Details
Envelope glycoprotein gp160P35961Details