Recently, the crystal structure of the N-terminal fragment of human Hsp90-alpha chaperone and its complex with geldanamycin and the crystal structure of the N-terminal domain of yeast Hsp90 have been determined at high resolution. These structures reveal features that shed new light on the Hsp90 chaperone–protein interactions.
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References
Gething, M-J. & Sambrook, J. Nature 355, 33–45 (1992).
Fenton, W.A. & Horwich, A.L. Protein Sci. 6, 743–760 (1997).
Martin, J. & Ultich-Hartl, F. Curr. Opin. Struct. Biol. 7, 41–52 (1997).
Ruddon, R.W. & Bedows, E. J. Biol. Chem. 272, 3125–3128 (1997).
Rutherford, S.L. & Zuker, C.S. Cell 79, 1129–1132 (1994).
Braig, K. et al. Nature 371, 578–586 (1994).
Buckle, A.M., Zahn, R. & Fersht, A.R. Proc. Natl. Acad. Sci. USA 94, 3571–3575 (1997).
Flaherty, K.M., DeLuca-Flaherty, C. & McKay, D.B. Nature 346, 623–628 (1990).
Sriram, M., Osipiuk, J., Freeman, B.C., Morimoto, R.I. & Joachimiak, A. Structure 5, 403–414 (1997).
Zhu, X. et al. Science 272, 1606–1614 (1996).
Jakob, U. & Buchner, J. TIBS 19, 205–211 (1994).
Bose, S., Weike, T., Bügl, H. & Buchner, J. Science 274, 1715–1717 (1996).
Freeman, B.C., Toft, D.O. & Morimoto, R.I. Science 274, 1718–1720 (1996).
Freeman, B.C. & Morimoto, R.I. EMBO J. 15, 2969–2979 (1996).
Yonehara, M., Minami, Y., Kawata, Y., Nagai, J. & Yahara I. J. Biol. Chem. 271, 2641–2645 (1996).
Bohen, S.P. & Yamamoto, K.R. The Biology of Heat Shock Proteins and Molecular Chaperones (eds Morimoto, R.I., Tissières, A. & Georgopoulos, C.) 313–334 (Cold Spring Harbor Laboratory Press, New York, 1994).
Whitesell, L., Mimnaugh, E.G., De Costa, B., Myers, C.E. & Neckers, L.M. Proc. Natl. Acad. Sci. USA 91, 8324–8328 (1994).
Smith, D.F. et al. Mol. Cell Biol. 15, 6804–6812 (1995).
Schneider, C., Sepp-Lorenzino, L., Nimmesgern, E., Ouerfelli, O., Danishefsky, S., Rosen, N. & Ulrich-Hartl, F. Proc Natl. Acad. Sci. USA 93, 14536–14541 (1996).
Bohen, S.P. & Yamamoto, K.R. Proc. Natl. Acad. Sci. USA 90, 11424–11428 (1993).
Cadepond, F et.al. Proc. Natl. Acad. Sci. USA 90, 10434–10438 (1993).
Jakob, U., Meyer, I., Bügl, H., André, S., Bardwell, J.C.A. & Buchner, J. J. Biol. Chem. 270, 14412–14419 (1995).
Jakob, U., Scheibel, T., Bose, S., Reinstein, J. & Buchner, J. J. Biol. Chem. 271, 10035–10041 (1996).
Wearsch, P.A. & Nicchitta, C.V. J. Biol. Chem. 272, 5152–5156 (1997).
Sullivan, W. et al. J. Biol. Chem. 272, 8007–8012 (1997).
Stebbins, C.E., Russo, A.A., Schneider, C., Rosen, N., Ulrigh-Hartl, F. & Pavletich, N.P. Cell 89, 239–250 (1997).
Prodromou, C., Roe, S.M., Piper, P.W. & Pearl, L.H. Nature Structural Biol. 477–482 (1997).
Owens-Grillo, J.K., Stancato, L.F., Hoffmann, I., Pratt, W.B. & Krishna, P. Biochemistry 35, 15249–15255 (1996).
Nieland, T.J.F. et al. Proc. Natl. Acad. Sci. USA 93, 6135–6139 (1996).
Fremont, D.H., Stura, E.A., Matsumura, M., Peterson, P.A. & Wilson, I.A. Proc. Nat. Acad. Sci. USA 92, 2479 (1995).
Stanfield, R.L. & Wilson, I.A. Curr. Opinion Structural Biol. 5, 103–113 (1995).
Tame, J.R.H. et al. Science 264, 1578–1581 (1994).
Fenton, W.A., Kashi, Y., Furtak, K. & Norwich, A.L. Nature 371, 614–619 (1994).
Keuhn, M.J. et al. Science 262, 1234–1241 (1993).
Madden, D.R., Gorga, J.C., Strominger, J.L. & Wiley, D.C. Cell 70, 1035–1048 (1992).
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Joachimiak, A. Capturing the misfolds: chaperone-peptide-binding motifs. Nat Struct Mol Biol 4, 430–434 (1997). https://doi.org/10.1038/nsb0697-430
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DOI: https://doi.org/10.1038/nsb0697-430