The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.
Crystal Structure of an Hsp90–Geldanamycin Complex: Targeting of a Protein Chaperone by an Antitumor Agent
Open accessAbstract
The Hsp90 chaperone is required for the activation of several families of eukaryotic protein kinases and nuclear hormone receptors, many of which are protooncogenic and play a prominent role in cancer. The geldanamycin antibiotic has antiproliferative and antitumor effects, as it binds to Hsp90, inhibits the Hsp90-mediated conformational maturation/refolding reaction, and results in the degradation of Hsp90 substrates. The structure of the geldanamycin-binding domain of Hsp90 (residues 9-232) reveals a pronounced pocket, 15 A deep, that is highly conserved across species. Geldanamycin binds inside this pocket, adopting a compact structure similar to that of a polypeptide chain in a turn conformation. This, and the pocket's similarity to substrate-binding sites, suggest that the pocket binds a portion of the polypeptide substrate and participates in the conformational maturation/refolding reaction.
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Cites
Whitesell, L., Mimnaugh, E. G., De Costa, B., Myers, C. E., & Neckers, L. M. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.18.8324 · Cited by 1,444
Reduced levels of hsp90 compromise steroid receptor action in vivo
Picard, D., Khursheed, B., Garabedian, M. J., Fortin, M. G., Lindquist, S., & Yamamoto, K. R. (1990) · Nature · doi:10.1038/348166a0 · Cited by 787 · cited 1×
“…in order to acquire orsimilarity to substrate-binding sites, suggest that the maintain a state competent to bind hormone (Bresnickpocket binds a portion of the polypeptide substrate et al., 1989; Picard et al., 1990; Nathan and Lindquist,and participates in the conformational maturation/ 1995).”
BackgroundBorkovich, K. A., Farrelly, F. W., Finkelstein, D. B., Taulien, J., & Lindquist, S. (1989) · Molecular and Cellular Biology · doi:10.1128/mcb.9.9.3919 · Cited by 641
Mammalian p50Cdc37 is a protein kinase-targeting subunit of Hsp90 that binds and stabilizes Cdk4
Stepanova, L., Leng, X., Parker, S. B., & Harper, J. W. (1996) · Genes & Development · doi:10.1101/gad.10.12.1491 · Cited by 483 · cited 2×
“…Hsp90GBD), and we determined the crystal structures of thiswith Hsp90 function and induces the rapid degradation of these kinases by the proteosome system (Murakami domain and of its complex with geldanamycin. et al., 1994; Schulte et al., 1995; Schneider et al., 1996; Stepanova et al., 1996).”
BackgroundMutational Analysis of Hsp90 Function: Interactions with a Steroid Receptor and a Protein Kinase
Nathan, D. F., & Lindquist, S. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.7.3917 · Cited by 423 · cited 1×
“…requirement for Hsp90 in the activation of the agent by the NCI (Supko et al., 1995). aforementioned protein kinases has been demonstrated both genetically (Xu and Lindquist, 1993; Aligue et al., 1994; Nathan and Lindquist, 1995) and biochemically‖ These authors contributed equally to this work.”
BackgroundHeat-shock protein hsp90 governs the activity of pp60v-src kinase.
Xu, Y., & Lindquist, S. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.15.7074 · Cited by 416 · cited 2×
“aforementioned protein kinases has been demonstrated both genetically (Xu and Lindquist, 1993; Aligue et al., 1994; Nathan and Lindquist, 1995) and biochemically ‖ These authors contributed equally to this work.”
Freeman, B. C., Toft, D. O., & Morimoto, R. I. (1996) · Science · doi:10.1126/science.274.5293.1718 · Cited by 370 · cited 1×
“…includes Hsp90, Hsp70, and several protein cofactors, such as Hsp70, which may contributeother cofactors is in equilibrium with the hormoneto polypeptide binding (Bose et al., 1996; Duina et al.,responsive state of the receptor, which is bound to 1996; Freeman et al., 1996; Schneider et al., 1996).”
BackgroundAligue, R., Akhavan‐Niak, H., & Russell, P. (1994) · The EMBO Journal · doi:10.1002/j.1460-2075.1994.tb06956.x · Cited by 261
Cited by
HSP90 and the chaperoning of cancer
Whitesell, L., & Lindquist, S. L. (2005) · Nature Reviews Cancer · doi:10.1038/nrc1716 · Cited by 2,502
HSP90 at the hub of protein homeostasis: emerging mechanistic insights
Taipale, M., Jarosz, D. F., & Lindquist, S. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2918 · Cited by 1,818
Schopf, F. H., Biebl, M. M., & Buchner, J. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.20 · Cited by 1,540
Induced protein degradation: an emerging drug discovery paradigm
Lai, A. C., & Crews, C. M. (2017) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2016.211 · Cited by 1,486
Paul Ehrlich's magic bullet concept: 100 years of progress
Strebhardt, K., & Ullrich, A. (2008) · Nature Reviews Cancer · doi:10.1038/nrc2394 · Cited by 1,457
Metadata
- Authors
- Stebbins, C. E., Russo, A. A., Schneider, C., Rosen, N., Hartl, F. U., & Pavletich, N. P.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1997-04
- Volume
- 89
- Issue
- 2
- Pages
- 239-250
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2139306838
- Cited by
- 1,364
- References
- 8
- FWCI
- 18.11
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Stebbins, C. E., Russo, A. A., Schneider, C., Rosen, N., Hartl, F. U., & Pavletich, N. P. (1997). Crystal Structure of an Hsp90–Geldanamycin Complex: Targeting of a Protein Chaperone by an Antitumor Agent. Cell. https://doi.org/10.1016/s0092-8674(00)80203-2
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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