Abstract
The crystal structure of interferon-γ bound to the extracellular fragment of its high-affinity cellsurface receptor reveals the first view of a class-2 cytokine receptor-ligand complex. In the complex, one interferon-γ homodimer binds two receptor molecules. Unlike the class-1 growth hormone receptor complex, the two interferon-γ receptors do not interact with one another and are separated by 27 Ã. Upon receptor binding, the flexible AB loop of interferon-γ undergoes a conformational change that includes the formation of a 310 helix.
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References
Farrar, M. A. & Schreiber, R. D. A. Rev. Immun. 11, 571–611 (1993).
Pestka, S., Lager, J. A., Zoon, K. C. & Samuel, C. E. Rev. Biochem. 56, 727–777 (1987).
Soh, J. et al. Proc. natn. Acad. Sci. U.S.A. 90, 8737–8741 (1993).
Jung, V. et al. Proc. natn. Acad. Sci. U.S.A. 84, 4151–4155 (1987).
Soh, J. et al. Cell 76, 793–802 (1994).
Hemmi, S., Bohni, R., Stark, G., Di Marco, F. & Aguet, M. Cell 76, 803–810 (1994).
Muller, M. et al. Nature 366, 129–135 (1993).
Darnell, J. E., Kerr, I. M. & Stark, G. R. Science 264, 1415–1421 (1994).
Aguet, M., Dembic, Z. & Merlin, G. Cell 55, 273–280 (1988).
Bazan, J. F. Proc. natn. Acad. Sci. U.S.A. 87, 6934–6938 (1990).
Ho, A. S. Y. et al. Proc. natn. Acad. Sci. U.S.A. 90, 11267–11271 (1993).
Uze, G., Lutfalla, G. & Gresser, I. Cell 60, 225–234 (1990).
Novick, D., Cohen, B. & Rubinstein, M. Cell 77, 391–400 (1994).
de Vos, A. M., Ultsch, M. & Kossiakoff, A. A. Science 255, 306–312 (1992).
Somers, W., Ultsch, M., De Vos, A. M. & Kossiakoff, A. A. Nature 372, 478–481 (1994).
Sprang, S. R. & Bazan, F. J. Curr. Opin. struct. Biol. 3, 815–827 (1993).
Ealick, S. E. et al. Science 252, 698–702 (1991).
Grzesiek, S. et al. Biochemistry 31, 8180–8190 (1992).
Harlos, K. et al. Nature 370, 662–666 (1994).
Muller, Y. A., Ultsch, M., Kelley, R. F. & de Vos, A. M. Biochemistry 33, 10864–10870 (1994).
Bork, P., Holm, L. & Sander, C. J. molec. Biol. 242, 309–320 (1994).
Jones, E. Y., Davis, S. J., Williams, A. F., Harlos, K. & Stuart, D. I. Nature 360, 232–239 (1992).
Wang, J. et al. Nature 348, 411–418 (1990).
Ryu, S. E. et al. Nature 348, 419–426 (1990).
Holmgren, A. & Bränden, C.-I. Nature 342, 248–251 (1989).
Kossiakoff, A. A. et al. Protein sci. 3, 1697–1705 (1994).
Griggs, N. D. et al. J. Immun. 149, 517–520 (1992).
Jarpe, M. A. & Johnson, H. M. J. Interfer. Res. 13, 99–103 (1993).
Lundell, D., Lunn, C. A., Senior, M. M., Zavodyn, P. J. & Narula, S. K. J. biol. Chem. 269, 16159–16162 (1994).
Lunn, C. A. et al. Protein Engng 5, 253–257 (1992).
Lundell, D. et al. Protein Engng 4, 335–341 (1991).
Wetzel, R., Perry, L. J., Veilleux, C. & Chang, G. Protein Engng 3, 611–623 (1990).
Manneberg, M., Friedlein, A., Kurth, H., Lahm, H-W. & Fountoulakis, M. Protein sci. 3, 30–38 (1994).
Rinderknect, E., O'Connor, B. H. & Rodriguez, H. J. biol. Chem. 259, 6790–6797 (1984).
Clackson, T. & Wells, J. A. Science 267, 383–386 (1995).
Hibino, Y., Kumar, C. S., Mariano, T. M., Lai, D. & Pestka, S. J. biol. Chem. 267, 3741–3749 (1992).
Lunn, C. A. et al. J. biol. Chem. 267, 17920–17924 (1992).
Otwinowski, Z. in Data Collection and Processing (eds Sawyer, L., Isaacs, N. & Bailey, S.) 56–62 (SERC Daresbury Laboratory, Warrington, 1993).
Collaborative Computational Project, 4 Acta crystallogr. D50, 760–763 (1994).
Navaza, J. Acta crystallogr. A50, 157–163 (1994).
Otwinowski, Z. in Isomorphous Replacement and Anomalous Scattering (eds Wolf, W., Evans, P. R. & Leslie, A. G. W.) 80–85 (SERC Daresbury Laboratory, Warrington, 1991).
Read, R. J. Acta crystallogr. A42, 140–159 (1986).
Wang, B. C. Meth Enzym. 115, 90–112 (1985).
Zhang, K. Y. & Main, P. Acta crystallogr. A46, 377–381 (1990).
Cowtan, K. in Jt CCP4 & ESF-EACBM Newsl. on Prot. Crystallogr. 31, 34–38 (1994).
Sack, J. S. J. molec. Graph. 6, 224–225 (1988).
Brünger, A. T. X-PLOR, Version 3.1, A System for X-ray Crystallography and NMR (Yale Univ. Press, New Haven, 1992).
Carson, M. J. appl. Crystallogr. 24, 958–961 (1991).
Connelly, M. L. J. molec. Graph. 11, 139–141 (1993).
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Walter, M., Windsor, W., Nagabhushan, T. et al. Crystal structure of a complex between interferon-γ and its soluble high-affinity receptor. Nature 376, 230–235 (1995). https://doi.org/10.1038/376230a0
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DOI: https://doi.org/10.1038/376230a0
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