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The structure of an intermediate in class II MHC maturation: CLIP bound to HLA-DR3
Naturevolume 378, pages457–462 (1995)Cite this article
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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.Nature360, 474–477 (1992).
Sette, A.et al.Science258, 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.Immunity1, 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.Nature368, 551–554 (1994).
Fling, S. P., Arp, B. & Pious, D.Nature368, 554–558 (1994).
Sloan, V. S.et al.Nature375, 802–806 (1995).
Denzin, L. K. & Cresswell, P.Cell82, 155–165 (1995).
Sherman, M. A., Weber, D. A. & Jensen, P. E.Immunity3, 197–205 (1995).
Mellins, E.et al.Nature343, 71–74 (1990).
Stern, L. J.et al.Nature368, 215–221 (1994).
Brown, J. H.et al.Nature368, 33–39 (1993).
Jardetzky, T. S.et al.Nature368, 711–718 (1994).
Kim, J., Urban, R. G., Strominger, J. L. & Wiley, D. C.Science266, 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.Cell68, 465–477 (1992).
Germain, R. N. & Rinker, A. G.Nature363, 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.Nature358, 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.Nature369, 120–126 (1994).
Nelson, C. A., Petzold, S. J. & Unanue, E. R.Nature371, 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.Nature355, 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. Graphics9, 230–236 (1991).
Nicholls, A., Sharp, K. A. & Honig, B.Proteins11, 281–296 (1991).
Kabsch, W.Acta crystallogr.A34, 827–828 (1978).
Madden, D. R., Gorga, J. C., Strominger, J. L. & Wiley, D. C.Cell70, 1035–1048 (1992).
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Department of Molecular and Cellular Biology, Harvard University, 7 Divinity Avenue, Cambridge, Massachusetts, 02138, USA
Partho Ghosh & Don C. Wiley
Howard Hughes Medical Institute, Harvard University, 7 Divinity Avenue, Cambridge, Massachusetts, 02138, USA
Don C. Wiley
Children's Hospital of Philadelphia and Children's Seashore House, Philadelphia, Pennsylvania, 19104, USA
Miguel Amaya & Elizabeth Mellins
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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.Nature378, 457–462 (1995). https://doi.org/10.1038/378457a0
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