Abstract
The CCR5 co-receptor binds to CD4-activated HIV-1 gp120 surface envelope glycoprotein and facilitates HIV-1 entry into cells. Key portions of CCR5 involved in gp120 binding include its N-terminus and second extra cellular loop (ECL2). The N-terminus of CCR5 contains multiple tyrosine-sulfate (Tyr-SO4) residues that are necessary for binding gp120, as do several antibodies that react with the co-receptor-binding site on gp120. We have used a combination of NMR spectroscopy, X-ray crystallography and molecular docking to solve the structure of the CCR5 N-terminus and the tyrosine-sulfated antibody, 412d, in complex with gp120 and CD4. These analyses have revealed a highly conserved Tyr-SO4-specific binding site on gp120 for which HIV-1 Entry inhibitors may be developed, and provide the structural basis for post-translational mimicry between the immune system and an HIV co-receptor. In ongoing studies we are using NMR and biochemical techniques to probe the interactions between CCR5's ECL-2 and gp120; results from these studies will also be discussed.
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