Structures of the CCR5 N terminus and of a tyrosine-sulfated antibody with HIV-1 gp120 and CD4.
Journal Article (Journal Article)
The CCR5 co-receptor binds to the HIV-1 gp120 envelope glycoprotein and facilitates HIV-1 entry into cells. Its N terminus is tyrosine-sulfated, as are many antibodies that react with the co-receptor binding site on gp120. We applied nuclear magnetic resonance and crystallographic techniques to analyze the structure of the CCR5 N terminus and that of the tyrosine-sulfated antibody 412d in complex with gp120 and CD4. The conformations of tyrosine-sulfated regions of CCR5 (alpha-helix) and 412d (extended loop) are surprisingly different. Nonetheless, a critical sulfotyrosine on CCR5 and on 412d induces similar structural rearrangements in gp120. These results now provide a framework for understanding HIV-1 interactions with the CCR5 N terminus during viral entry and define a conserved site on gp120, whose recognition of sulfotyrosine engenders posttranslational mimicry by the immune system.
Full Text
Duke Authors
Cited Authors
- Huang, C-C; Lam, SN; Acharya, P; Tang, M; Xiang, S-H; Hussan, SS-U; Stanfield, RL; Robinson, J; Sodroski, J; Wilson, IA; Wyatt, R; Bewley, CA; Kwong, PD
Published Date
- September 28, 2007
Published In
Volume / Issue
- 317 / 5846
Start / End Page
- 1930 - 1934
PubMed ID
- 17901336
Pubmed Central ID
- PMC2278242
Electronic International Standard Serial Number (EISSN)
- 1095-9203
Digital Object Identifier (DOI)
- 10.1126/science.1145373
Language
- eng
Conference Location
- United States