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Structure of the CCR5 Chemokine Receptor–HIV Entry Inhibitor Maraviroc Complex
Open accessAbstract
CCR5-Maraviroc Structure: The chemokine receptor CCR5, a G protein–coupled receptor best known as a co-receptor during HIV-1 infection, is important in a variety of physiological processes. Tan et al. (p. 1387 , published online 12 September; see the Perspective by Klasse ) now report the high-resolution crystal structure of CCR5 bound to the HIV-1 entry inhibitor, Maraviroc. The structure suggests that Maraviroc acts as a noncompetitive inhibitor by binding to a region of CCR5 that is distinct from the binding site of HIV-1 and chemokines. Comparison of the structure of CCR5 with the other HIV-1 co-receptor, the chemokine receptor CXCR4, provides insight into the co-receptor selectivity of the virus.
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[20] Processing of X-ray diffraction data collected in oscillation mode
Otwinowski, Z., & Minor, W. (1997) · Methods in Enzymology · doi:10.1016/s0076-6879(97)76066-x · Cited by 33,475
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McCoy, A. J., Grosse-Kunstleve, R. W., Adams, P. D., Winn, M. D., Storoni, L. C., & Read, R. J. (2007) · Journal of Applied Crystallography · doi:10.1107/s0021889807021206 · Cited by 20,612
Crystal Structure of Rhodopsin: A G Protein-Coupled Receptor
Palczewski, K., Kumasaka, T., Hori, T., Behnke, C. A., Motoshima, H., Fox, B. A., Trong, I. L., Teller, D. C., Okada, T., Stenkamp, R. E., et al. (2000) · Science · doi:10.1126/science.289.5480.739 · Cited by 5,637
Crystal structure of the β2 adrenergic receptor–Gs protein complex
Rasmussen, S. G. F., DeVree, B. T., Zou, Y., Kruse, A. C., Chung, K. Y., Kobilka, T. S., Thian, F. S., Chae, P. S., Pardon, E., Calinski, D., et al. (2011) · Nature · doi:10.1038/nature10361 · Cited by 3,009
Chemokine receptors as HIV-1 coreceptors: roles in viral entry, tropism, and disease
Berger, E. A., Murphy, P. M., & Farber, J. M. (1999) · Annual Review of Immunology · doi:10.1146/annurev.immunol.17.1.657 · Cited by 2,180
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Metadata
- Authors
- Tan, Q., Zhu, Y., Li, J., Chen, Z., Han, G. W., Kufareva, I., Li, T., Ma, L., Fenalti, G., Li, J., Zhang, W., Xie, X., Yang, H., Jiang, H., Cherezov, V., Liu, H., Stevens, R. C., Zhao, Q., & Wu, B.
- Venue
- Science
- Published
- 2013-09-20
- Volume
- 341
- Issue
- 6152
- Pages
- 1387-1390
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2146933058
- Cited by
- 712
- References
- 5
- FWCI
- 42.84
- Type
- journal article
- Language
- en
- Open access
- green
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- Tan, Q., Zhu, Y., Li, J., Chen, Z., Han, G. W., Kufareva, I., Li, T., Ma, L., Fenalti, G., Li, J., Zhang, W., Xie, X., Yang, H., Jiang, H., Cherezov, V., Liu, H., Stevens, R. C., Zhao, Q., & Wu, B. (2013). Structure of the CCR5 Chemokine Receptor–HIV Entry Inhibitor Maraviroc Complex. Science. https://doi.org/10.1126/science.1241475
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