Abstract
A complex between HLA-DR3 and a fragment of invariant chain called CLIP was isolated from a human cell line defective in antigen presentation and its X-ray crystal structure determined. Previous data indicate that this complex is an intermediate in class II histocompatibility maturation, occurring between invariant chain–DR3 and antigenic peptide–DR3 complexes. The structure shows that the CLIP fragment binds to DR3 in a way almost identical to that in which antigenic peptides bind class II histocompatibility gly cop rote ins. The structure is the substrate for the loading of antigenic peptides by an exchange process catalysed by DM.
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References
Cresswell, P. A. Rev. Immun. 12, 259–293 (1994).
Riberdy, J. M., Newcomb, J. R., Surman, M. J., Barbosa, J. A. & Cresswell, P. Nature 360, 474–477 (1992).
Sette, A. et al. Science 258, 1801–1804 (1992).
Mellins, E. et al. J. exp. Med. 179, 541–549 (1994).
Monji, T., McCormack, A. L., Yates, J. R. & Pious, D. J. exp. Med. 153, 4468–4477 (1994).
Avva, R. & Cresswell, P. Immunity 1, 763–774 (1994).
Xu, M., Capraro, G. A., Daibata, M., Reyes, V. E. & Humphreys, R. E. Molec. Immun. 31, 723–731 (1994).
Freisewinkel, I. M., Schenck, K. & Koch, N. Proc. natn. Acad. Sci. U.S.A. 90, 9703–9706 (1993).
Romagnoli, P. & Germain, R. N. J. exp. Med. 180, 1107–1113 (1994).
Bijlmakers, M. E., Benaroch, P. & Ploegh, H. L. J. exp. Med. 180, 623–629 (1994).
Malcherek, G., Gnau, V., Jung, G., Rammensee, H.-G. & Melms, A. J. exp. Med. 181, 527–536 (1995).
Sette, A., Southwood, S., Miller, J. & Apella, E. J. exp. Med. 181, 677–683 (1995).
Geluk, A., van Meijgaarden, K. E., Drijfhout, J. W. & Ottenhof, T. H. M. Molec. Immun. 32, 975–981 (1995).
Gautam, A. N., Pearson, C., Quinn, V., McDevitt, H. O. & Milburn, P. J. Proc. natn. Acad. Sci. U.S.A. 92, 335–339 (1995).
Kropshofer, H., Vogt, A. B. & Hämmerling, G. J. Proc. natn. Acad. Sci. U.S.A. 92, 8313–8317 (1995).
Morris, P. et al. Nature 368, 551–554 (1994).
Fling, S. P., Arp, B. & Pious, D. Nature 368, 554–558 (1994).
Sloan, V. S. et al. Nature 375, 802–806 (1995).
Denzin, L. K. & Cresswell, P. Cell 82, 155–165 (1995).
Sherman, M. A., Weber, D. A. & Jensen, P. E. Immunity 3, 197–205 (1995).
Mellins, E. et al. Nature 343, 71–74 (1990).
Stern, L. J. et al. Nature 368, 215–221 (1994).
Brown, J. H. et al. Nature 368, 33–39 (1993).
Jardetzky, T. S. et al. Nature 368, 711–718 (1994).
Kim, J., Urban, R. G., Strominger, J. L. & Wiley, D. C. Science 266, 1870–1874 (1994).
Urban, R. G., Chicz, R. M. & Strominger, J. L. J. exp. Med. 180, 751–755 (1994).
Malcherek, G. et al. Int. Immun. 5, 1229–1237 (1993).
Geluk, A. et al. J. Immun. 152, 5742–5748 (1994).
Stern, L. J. & Wiley, D. C. Cell 68, 465–477 (1992).
Germain, R. N. & Rinker, A. G. Nature 363, 725–728 (1993).
Morkowski, S. et al. J. exp. Med. 182, 1403–1413 (1995).
Jasanoff, A., Park, S.-J. & Wiley, D. C. Proc. natn. Acad. Sci. U.S.A. 92, 9900–9904 (1995).
Park, S.-J., Sadegh-Nasseri, S. & Wiley, D. C. Proc. natn. Acad. Sci. U.S.A. 92, 11289–11293 (1995).
Lee, C. & McConnell, H. Proc. natn. Acad. Sci. U.S.A. 92, 8269–8273 (1995).
Chicz, R. M. et al. Nature 358, 764–768 (1992).
Chicz, R. M. et al. J. exp. Med. 178, 27–47 (1993).
Tulp, A., Verwoerd, D., Dobberstein, B., Ploegh, H. L. & Pieters, J. Nature 369, 120–126 (1994).
Nelson, C. A., Petzold, S. J. & Unanue, E. R. Nature 371, 250–252 (1994).
Maurer, D. & Gorski, J. J. Immun. 146, 621–626 (1991).
Gorga, J. C., Horejsi, V., Johnson, D. R., Raghupathy, R. & Strominger, J. L. J. biol. Chem. 262, 16087–16094 (1987).
Gorga, J. C., Brown, J. H., Jardetzky, T., Wiley, D. C. & Strominger, J. L. Res. Immun. 142, 401–407 (1991).
Collaborative Computational Project, N. Acta crystallogr. D50, 760–763 (1994).
Navaza, J. Acta crystallogr. A50, 157–163 (1994).
Brünger, A. T. Nature 355, 472–475 (1992).
Jones, T. A., Zou, J.-Y., Cowan, S. W. & Kjeldgaard, M. Acta crystallogr. A47, 110–119 (1991).
Luzzati, V. Acta crystallogr. 5, 802–810 (1952).
Huang, C. C., Petterson, E. F., Klein, T. E., Ferrin, T. E. & Langridge, R. J. molec. Graphics 9, 230–236 (1991).
Nicholls, A., Sharp, K. A. & Honig, B. Proteins 11, 281–296 (1991).
Kabsch, W. Acta crystallogr. A34, 827–828 (1978).
Madden, D. R., Gorga, J. C., Strominger, J. L. & Wiley, D. C. Cell 70, 1035–1048 (1992).
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Ghosh, P., Amaya, M., Mellins, E. et al. The structure of an intermediate in class II MHC maturation: CLIP bound to HLA-DR3. Nature 378, 457–462 (1995). https://doi.org/10.1038/378457a0
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DOI: https://doi.org/10.1038/378457a0
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