Crystal structure of an Hsp90–nucleotide–p23/Sba1 closed chaperone complex (original) (raw)

• Panaretou, B. et al. ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo. EMBO J. 17, 4829–4836 (1998)
  CAS PubMed PubMed Central Google Scholar
• Obermann, W. M. J., Sondermann, H., Russo, A. A., Pavletich, N. P. & Hartl, F. U. In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis. J. Cell Biol. 143, 901–910 (1998)
  CAS PubMed PubMed Central Google Scholar
• Mimnaugh, E. G., Chavany, C. & Neckers, L. Polyubiquitination and proteasomal degradation of the p185c-erbB-2 receptor protein-tyrosine kinase induced by geldanamycin. J. Biol. Chem. 271, 22796–22801 (1996)
  CAS PubMed Google Scholar
• Schneider, C. et al. Pharmacologic shifting of a balance between protein folding and degradation mediated by Hsp90. Proc. Natl Acad. Sci. USA 93, 14536–14541 (1996)
  ADS CAS PubMed PubMed Central Google Scholar
• Pearl, L. H. Hsp90 and Cdc37—a chaperone cancer conspiracy. Curr. Opin. Genet. Dev. 15, 55–61 (2005)
  CAS PubMed Google Scholar
• Workman, P. Combinatorial attack on multistep oncogenesis by inhibiting the Hsp90 molecular chaperone. Cancer Lett. 206, 149–157 (2004)
  CAS PubMed Google Scholar
• Panaretou, B. et al. Activation of the ATPase activity of Hsp90 by the stress-regulated co-chaperone Aha1. Mol. Cell 10, 1307–1318 (2002)
  CAS PubMed Google Scholar
• Prodromou, C. et al. Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)-domain co-chaperones. EMBO J. 18, 754–762 (1999)
  CAS PubMed PubMed Central Google Scholar
• Siligardi, G. et al. Regulation of Hsp90 ATPase activity by the co-chaperone Cdc37p/p50cdc37. J. Biol. Chem. 277, 20151–20159 (2002)
  CAS PubMed Google Scholar
• Johnson, J. L. & Toft, D. O. Binding of p23 and hsp90 during assembly with the progesterone receptor. Mol. Endocrinol. 9, 670–678 (1995)
  CAS PubMed Google Scholar
• Fang, Y., Fliss, A. E., Rao, J. & Caplan, A. J. SBA1 encodes a yeast hsp90 cochaperone that is homologous to vertebrate p23 proteins. Mol. Cell. Biol. 18, 3727–3734 (1998)
  CAS PubMed PubMed Central Google Scholar
• Sullivan, W. et al. Nucleotides and two functional states of hsp90. J. Biol. Chem. 272, 8007–8012 (1997)
  CAS PubMed Google Scholar
• Siligardi, G. et al. Co-chaperone regulation of conformational switching in the Hsp90 ATPase cycle. J. Biol. Chem. 279, 51989–51998 (2004)
  CAS PubMed Google Scholar
• McLaughlin, S. H., Smith, H. W. & Jackson, S. E. Stimulation of the weak ATPase activity of human Hsp90 by a client protein. J. Mol. Biol. 315, 787–798 (2002)
  CAS PubMed Google Scholar
• Richter, K., Walter, S. & Buchner, J. The co-chaperone Sba1 connects the ATPase reaction of Hsp90 to the progression of the chaperone cycle. J. Mol. Biol. 342, 1403–1413 (2004)
  CAS PubMed Google Scholar
• Pratt, W. B. & Dittmar, K. D. Studies with purified chaperones advance the understanding of the mechanism of glucocorticoid receptor hsp90 heterocomplex assembly. Trends Endocrinol. Metab. 9, 244–252 (1998)
  CAS PubMed Google Scholar
• Young, J. C. & Hartl, F. U. Polypeptide release by Hsp90 involves ATP hydrolysis and is enhanced by the co-chaperone p23. EMBO J. 19, 5930–5940 (2000)
  CAS PubMed PubMed Central Google Scholar
• Chadli, A. et al. Dimerization and N-terminal domain proximity underlie the function of the molecular chaperone heat shock protein 90. Proc. Natl Acad. Sci. USA 97, 12524–12529 (2000)
  ADS CAS PubMed PubMed Central Google Scholar
• Prodromou, C. et al. The ATPase cycle of Hsp90 drives a molecular ‘clamp’ via transient dimerization of the N-terminal domains. EMBO J. 19, 4383–4392 (2000)
  CAS PubMed PubMed Central Google Scholar
• Huai, Q. et al. Structures of the N-terminal and middle domains of E. coli Hsp90 and conformation changes upon ADP binding. Structure 13, 579–590 (2005)
  CAS PubMed Google Scholar
• Immormino, R. M. et al. Ligand-induced conformational shift in the N-terminal domain of GRP94, an Hsp90 chaperone. J. Biol. Chem. 279, 46162–46171 (2004)
  CAS PubMed Google Scholar
• McLaughlin, S. H., Ventouras, L. A., Lobbezoo, B. & Jackson, S. E. Independent ATPase activity of Hsp90 subunits creates a flexible assembly platform. J. Mol. Biol. 344, 813–826 (2004)
  CAS PubMed Google Scholar
• Louvion, J. F., Warth, R. & Picard, D. Two eukaryote-specific regions of Hsp82 are dispensable for its viability and signal transduction functions in yeast. Proc. Natl Acad. Sci. USA 93, 13937–13942 (1996)
  ADS CAS PubMed PubMed Central Google Scholar
• Prodromou, C., Roe, S. M., Piper, P. W. & Pearl, L. H. A molecular clamp in the crystal structure of the N-terminal domain of the yeast Hsp90 chaperone. Nature Struct. Biol. 4, 477–482 (1997)
  CAS PubMed Google Scholar
• Meyer, P. et al. Structural and functional analysis of the middle segment of Hsp90: Implications for ATP hydrolysis and client-protein and co-chaperone interactions. Mol. Cell 11, 647–658 (2003)
  CAS PubMed Google Scholar
• Weaver, A. J., Sullivan, W. P., Felts, S. J., Owen, B. A. & Toft, D. O. Crystal structure and activity of human p23, a heat shock protein 90 co-chaperone. J. Biol. Chem. 275, 23045–23052 (2000)
  CAS PubMed Google Scholar
• Prodromou, C. et al. Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone. Cell 90, 65–75 (1997)
  CAS PubMed Google Scholar
• Stebbins, C. E. et al. Crystal structure of an Hsp90-geldanamycin complex: Targetting of a protein chaperone by an antitumor agent. Cell 89, 239–250 (1997)
  CAS PubMed Google Scholar
• Roe, S. M. et al. The structural basis for inhibition of the Hsp90 molecular chaperone, by the anti-tumour antibiotics radicicol and geldanamycin. J. Med. Chem. 42, 260–266 (1999)
  CAS PubMed Google Scholar
• Cheung, K. M. et al. The identification, synthesis, protein crystal structure and in vitro biochemical evaluation of a new 3,4-diarylpyrazole class of Hsp90 inhibitors. Bioorg. Med. Chem. Lett. 15, 3338–3343 (2005)
  ADS CAS PubMed Google Scholar
• Wright, L. et al. Structure-activity relationships in purine-based inhibitor binding to HSP90 isoforms. Chem. Biol. 11, 775–785 (2004)
  CAS PubMed Google Scholar
• Harris, S. F., Shiau, A. K. & Agard, D. A. The crystal structure of the carboxy-terminal dimerization domain of htpG, the Escherichia coli Hsp90, reveals a potential substrate binding site. Structure 12, 1087–1097 (2004)
  CAS PubMed Google Scholar
• Scheufler, C. et al. Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine. Cell 101, 199–210 (2000)
  CAS PubMed Google Scholar
• Bohen, S. P. & Yamamoto, K. R. Isolation of Hsp90 mutants by screening for decreased steroid receptor function. Proc. Natl Acad. Sci. USA 90, 11424–11428 (1993)
  ADS CAS PubMed PubMed Central Google Scholar
• Nathan, D. F. & Lindquist, S. Mutational analysis of Hsp90 function: interactions with a steroid receptor and a protein kinase. Mol. Cell. Biol. 15, 3917–3925 (1995)
  CAS PubMed PubMed Central Google Scholar
• Ban, C., Junop, M. & Yang, W. Transformation of MutL by ATP binding and hydrolysis: a switch in DNA mismatch repair. Cell 97, 85–97 (1999)
  CAS PubMed Google Scholar
• Wigley, D. B., Davies, G. J., Dodson, E. J., Maxwell, A. & Dodson, G. Crystal structure of an N-terminal fragment of the DNA gyrase B protein. Nature 351, 624–629 (1991)
  ADS CAS PubMed Google Scholar
• Meyer, P. et al. Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery. EMBO J. 23, 511–519 (2004)
  CAS PubMed PubMed Central Google Scholar
• Oxelmark, E. et al. Genetic dissection of p23, an Hsp90 cochaperone, reveals a distinct surface involved in estrogen receptor signaling. J. Biol. Chem. 278, 36547–36555 (2003)
  CAS PubMed Google Scholar
• Lotz, G. P., Lin, H., Harst, A. & Obermann, W. M. J. Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone. J. Biol. Chem. 278, 17228–17235 (2003)
  CAS PubMed Google Scholar
• Harst, A., Lin, H. & Obermann, W. M. Aha1 competes with Hop, p50 and p23 for binding to the molecular chaperone Hsp90 and contributes to kinase and hormone receptor activation. Biochem. J. 387, 789–796 (2005)
  CAS PubMed PubMed Central Google Scholar
• Zhang, W. et al. Biochemical and structural studies of the interaction of Cdc37 with Hsp90. J. Mol. Biol. 340, 891–907 (2004)
  CAS PubMed Google Scholar
• Richter, K., Reinstein, J. & Buchner, J. N-terminal residues regulate the catalytic efficiency of the Hsp90 ATPase cycle. J. Biol. Chem. 277, 44905–44910 (2002)
  CAS PubMed Google Scholar
• Roe, S. M. et al. The mechanism of Hsp90 regulation by the protein kinase-specific cochaperone p50cdc37. Cell 116, 87–98 (2004)
  CAS PubMed Google Scholar