The DOI matches its Crossref record; 79 of the 79 references it cites were found in a registry or an index.
Structures of the CCR5 N Terminus and of a Tyrosine-Sulfated Antibody with HIV-1 gp120 and CD4
Open accessAbstract
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 (α-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.
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Metadata
- Authors
- Huang, C.-C., Lam, S. N., Acharya, P., Tang, M., Xiang, S.-H., Hussan, S. S.-U., Stanfield, R. L., Robinson, J., Sodroski, J., Wilson, I. A., Wyatt, R., Bewley, C. A., & Kwong, P. D.
- Venue
- Science
- Published
- 2007-09-28
- Volume
- 317
- Issue
- 5846
- Pages
- 1930-1934
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2024011553
- Cited by
- 416
- References
- 79
- FWCI
- 12.68
- Type
- journal article
- Language
- en
- Open access
- green
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- Huang, C.-C., Lam, S. N., Acharya, P., Tang, M., Xiang, S.-H., Hussan, S. S.-U., Stanfield, R. L., Robinson, J., Sodroski, J., Wilson, I. A., Wyatt, R., Bewley, C. A., & Kwong, P. D. (2007). Structures of the CCR5 N Terminus and of a Tyrosine-Sulfated Antibody with HIV-1 gp120 and CD4. Science. https://doi.org/10.1126/science.1145373
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